Plasma insulin concentrations and amino acid turnover in Merino sheep with high or low fleece weight

2004 ◽  
Vol 55 (8) ◽  
pp. 833 ◽  
Author(s):  
N. R. Adams ◽  
S. M. Liu ◽  
J. R. Briegel ◽  
M. J. Thompson
Keyword(s):  
Amino Acids ◽  
Plasma Insulin ◽  
Plasma Concentrations ◽  
Amino Nitrogen ◽  
Whole Body ◽  
Metabolic Demand ◽  
Body Protein ◽  
Wool Growth ◽  
Staple Strength ◽  
Fleece Weight

Although sheep with a relatively high fleece weight have reduced fat deposition and a lower reproductive rate, research has failed to identify any specific metabolic demand that growing a fleece places on the physiology of the sheep. This paper reports two experiments in which the effect of fleece weight was examined in ewes infused intravenously with amino acids. The first experiment was carried out when the ewes were 107 days pregnant, and the second 2 years later in non-pregnant ewes from the same flock. The ewes were derived initially from groups that differed in staple strength, but there was no effect of staple strength group on the characteristics measured in either experiment. In Expt 2, ewes were also infused with a bolus of l-[ring-d5] phenylalanine, and the enrichment in plasma determined by GC/mass spectrometry over the next 24 h. In both experiments, fasting plasma insulin concentrations were lower (P < 0.05) in ewes with a high fleece weight, and this difference continued during infusion in Expt 2 (P < 0.05). In Expt 1, infusion of ewes with amino acids resulted in higher (P < 0.05) plasma concentrations of α-amino nitrogen (indicating amino acids) in the ewes with a higher fleece weight, and in Expt 2, ewes with a high fleece weight had a 19% higher rate of appearance of endogenous phenylalanine (P < 0.05). We conclude that sheep with high wool growth rates have higher whole-body protein turnover rate, which may be achieved in part by lower insulin concentrations. Lower insulin in turn provides a mechanism through which wool growth rate may influence energy availability to other tissues.

Effect of glucose or amino acid infusion during pregnancy in ewes with different wool growth responsiveness to nutrition

2004 ◽  
Vol 55 (1) ◽  
pp. 47 ◽  
Author(s):  
M. J. Thompson ◽  
J. R. Briegel ◽  
N. R. Adams
Keyword(s):  
Amino Acids ◽  
Plasma Concentrations ◽  
Amino Nitrogen ◽  
Insulin Response ◽  
Late Pregnancy ◽  
Glucose Infusion ◽  
Control Line ◽  
Amino Acid Infusion ◽  
Wool Growth ◽  
Staple Strength

The reason why wool growth is suppressed in pregnancy is unclear. The present study examined the response to the nutrient drains imposed by pregnancy in 3 genotypes that had been selected for low (SS–) or high (SS+) staple strength, and a random control line. These flocks differ in the responsiveness of their protein metabolism to nutrient supply. Three groups of 20 pregnant ewes were fed to maintain conceptus-free liveweight, and were challenged with an infusion of glucose or amino acids in mid (Day 104) or late (Day 138) pregnancy. Infusion of glucose in late pregnancy caused a lower increment in plasma glucose concentration (P < 0.001) compared with mid-pregnancy, whereas plasma insulin responses to glucose infusion were not significantly different across time. In contrast, infusion of amino acids caused a greater increase in plasma concentrations of α-amino nitrogen in all genotypes in late pregnancy (P < 0.01), whereas the insulin response to amino acids was reduced (P < 0.001). Despite slower clearance of amino acids and decreased wool protein synthesis, the concentrations of blood urea nitrogen (BUN) were elevated in late pregnancy. The genotypes did not differ in their response to infusion with amino acids, but the SS– genotype had higher basal glucose and insulin concentrations. We conclude that the suppression in wool growth as pregnancy progresses was accompanied by greater oxidation but slower clearance of amino acids from plasma, associated with a lower insulin response. This defect in insulin response was selective for amino acids, because it was not observed in response to glucose infusion.

scholarly journals The impact of Hayward green kiwifruit on dietary protein digestion and protein metabolism

2020 ◽  
Author(s):  
Sanghee Park ◽  
David D. Church ◽  
Carlene Starck ◽  
Scott E. Schutzler ◽  
Gohar Azhar ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dietary Protein ◽  
Protein Metabolism ◽  
Plasma Concentrations ◽  
Whole Body ◽  
Protein Digestion ◽  
Body Protein ◽  
Before And After ◽  
The Impact ◽  
Green Kiwifruit

Abstract Purpose The purpose of the study was to determine if an actinidin protease aids gastric digestion and the protein anabolic response to dietary protein. Methods Hayward green kiwifruit (containing an actinidin protease) and Hort 16A gold kiwifruit (devoid of actinidin protease) were given in conjunction with a beef meal to healthy older subjects. Twelve healthy older males (N = 6) and females (N = 6) were studied with a randomized, double-blinded, crossover design to assess muscle and whole-body protein metabolism before and after ingestion of kiwifruit and 100 g of ground beef. Subjects consumed 2 of each variety of kiwifruit daily for 14 d prior to each metabolic study, and again during each study with beef intake. Results Hayward green kiwifruit consumption with beef resulted in a more rapid increase in peripheral plasma essential amino acid concentrations. There were significant time by kiwifruit intake interactions for plasma concentrations of EAAs, branched chain amino acids (BCAAs), and leucine (P < 0.01). However, there was no difference in the total amount of EAAs absorbed. As a result, there were no differences between kiwifruit in any of the measured parameters of protein kinetics. Conclusion Consumption of Hayward green kiwifruit, with a beef meal facilitates protein digestion and absorption of the constituent amino acids as compared to Hort 16A gold kiwifruit. Clinical trial NCT04356573, April 21, 2020 “retrospectively registered”.

Aspects of protein metabolism after elective surgery in patients receiving constant nutritional support

1990 ◽  
Vol 78 (6) ◽  
pp. 621-628 ◽  
Author(s):  
F. Carli ◽  
J. Webster ◽  
V. Ramachandra ◽  
M. Pearson ◽  
M. Read ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Metabolic Rate ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Resting Metabolic Rate ◽  
Plasma Concentrations ◽  
Whole Body ◽  
Body Protein ◽  
Urinary Nitrogen

1. The present study was designed in an attempt to resolve conflicting views currently in the literature relating to the effect of surgery on various aspects of protein metabolism. 2. Sequential post-operative (2, 4 and 6 days) changes in whole-body protein turnover, forearm arteriovenous difference of plasma amino acids, glucose, lactate and free fatty acids, muscle concentration of free amino acids, RNA and protein, urinary nitrogen and 3-methylhistidine, plasma concentrations of insulin, cortisol and growth hormone, and resting metabolic rate, were measured in six patients undergoing uncomplicated elective total abdominal hysterectomy. 3. All patients received a constant daily diet, either orally or intravenously, based on 0.1 g of nitrogen/kg and an energy content of 1.1 times the resting metabolic rate for 7 days before and 6 days after surgery. 4. Whole-body protein turnover, synthesis and breakdown increased significantly 2 days after surgery (P <0.05) and returned towards pre-operative levels thereafter. 5. Forearm release of branched-chain amino acids and alanine, and efflux of glucose and lactate, were enhanced 4 days after surgery (P <0.05). Muscle glutamine and alanine concentrations were decreased on the fourth and sixth days after surgery (P <0.05). The RNA/protein ratio (indicating the capacity for protein synthesis) was unaltered. 6. A significant increase in urinary nitrogen and 3-methylhistidine was observed on days 3 and 4 after surgery (P <0.05). Thereafter, these parameters remained elevated, although failing to reach statistical significance. 7. The resting metabolic rate was significantly increased (P <0.05) 2 days after surgery but the respiratory quotient (0.77) was unchanged. 8. These data support the contention that whole-body protein synthesis and breakdown increase after surgery. Differences observed pre- and post-operatively between leucine kinetic estimates and other methods of quantifying protein metabolism indicate that only like methodologies should be compared.

Measurement of protein turnover in the small intestine of lambs. 2. Effects of feed intake

1997 ◽  
Vol 128 (2) ◽  
pp. 233-246 ◽  
Author(s):  
S. A. NEUTZE ◽  
J. M. GOODEN ◽  
V. H. ODDY
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Small Intestine ◽  
Experimental Model ◽  
Feed Intake ◽  
Protein Turnover ◽  
Jugular Vein ◽  
Specific Radioactivity ◽  
Whole Body ◽  
Body Protein

This study used an experimental model, described in a companion paper, to examine the effects of feed intake on protein turnover in the small intestine of lambs. Ten male castrate lambs (∼ 10 months old) were offered, via continuous feeders, either 400 (n = 5) or 1200 (n = 5) g/day lucerne chaff, and mean experimental liveweights were 28 and 33 kg respectively. All lambs were prepared with catheters in the cranial mesenteric vein (CMV), femoral artery (FA), jugular vein and abomasum, and a blood flow probe around the CMV. Cr-EDTA (0·139 mg Cr/ml, ∼ 0·2 ml/min) was infused abomasally for 24 h and L-[2,6-3H]phenylalanine (Phe) (420±9·35 μCi into the abomasum) and L-[U-14C]phenylalanine (49·6±3·59 μCi into the jugular vein) were also infused during the last 8 h. Blood from the CMV and FA was sampled during the isotope infusions. At the end of infusions, lambs were killed and tissue (n = 4) and digesta (n = 2) samples removed from the small intestine (SI) of each animal. Transfers of labelled and unlabelled Phe were measured between SI tissue, its lumen and blood, enabling both fractional and absolute rates of protein synthesis and gain to be estimated.Total SI mass increased significantly with feed intake (P < 0·05), although not on a liveweight basis. Fractional rates of protein gain in the SI tended to increase (P = 0·12) with feed intake; these rates were −16·2 (±13·7) and 23·3 (±15·2) % per day in lambs offered 400 and 1200 g/day respectively. Mean protein synthesis and fractional synthesis rates (FSR), calculated from the mean retention of 14C and 3H in SI tissue, were both positively affected by feed intake (0·01 < P < 0·05). The choice of free Phe pool for estimating precursor specific radioactivity (SRA) for protein synthesis had a major effect on FSR. Assuming that tissue free Phe SRA represented precursor SRA, mean FSR were 81 (±15) and 145 (±24) % per day in lambs offered 400 and 1200 g/day respectively. Corresponding estimates for free Phe SRA in the FA and CMV were 28 (±2·9) and 42 (±3·5) % per day on 400 g/day, and 61 (±2·9) and 94 (±6·0) on 1200 g/day. The correct value for protein synthesis was therefore in doubt, although indirect evidence suggested that blood SRA (either FA or CMV) may be closest to true precursor SRA. This evidence included (i) comparison with flooding dose estimates of FSR, (ii) comparison of 3H[ratio ]14C Phe SRA in free Phe pools with this ratio in SI protein, and (iii) the proportion of SI energy use associated with protein synthesis.Using the experimental model, the proportion of small intestinal protein synthesis exported was estimated as 0·13–0·27 (depending on the choice of precursor) and was unaffected by feed intake. The contribution of the small intestine to whole body protein synthesis tended to be higher in lambs offered 1200 g/day (0·21) than in those offered 400 g/day (0·13). The data obtained in this study suggested a role for the small intestine in modulating amino acid supply with changes in feed intake. At high intake (1200 g/day), the small intestine increases in mass and CMV uptake of amino acids is less than absorption from the lumen, while at low intake (400 g/day), this organ loses mass and CMV uptake of amino acids exceeds that absorbed. The implications of these findings are discussed.

scholarly journals Presleep dietary protein-derived amino acids are incorporated in myofibrillar protein during postexercise overnight recovery

2018 ◽  
Vol 314 (5) ◽  
pp. E457-E467 ◽  
Author(s):  
Jorn Trommelen ◽  
Imre W. K. Kouw ◽  
Andrew M. Holwerda ◽  
Tim Snijders ◽  
Shona L. Halson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Dietary Protein ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Body Protein ◽  
Protein Ingestion ◽  
Casein Protein ◽  
The Impact ◽  
Myofibrillar Protein Synthesis

The purpose of this study was to determine the impact of ingesting 30 g casein protein with and without 2 g free leucine before sleep on myofibrillar protein synthesis rates during postexercise overnight recovery. Thirty-six healthy young men performed a single bout of resistance-type exercise in the evening (1945) after a full day of dietary standardization. Thirty minutes before sleep (2330), subjects ingested 30 g intrinsically l-[1-13C]phenylalanine-labeled protein with (PRO+leu, n = 12) or without (PRO, n = 12) 2 g free leucine, or a noncaloric placebo (PLA, n = 12). Continuous intravenous l-[ ring-2H5]phenylalanine, l-[1-13C]leucine, and l-[ ring-2H2]tyrosine infusions were applied. Blood and muscle tissue samples were collected to assess whole body protein net balance, myofibrillar protein synthesis rates, and overnight incorporation of dietary protein-derived amino acids into myofibrillar protein. Protein ingestion before sleep improved overnight whole body protein net balance ( P < 0.001). Myofibrillar protein synthesis rates did not differ significantly between treatments as assessed by l-[ ring-2H5]phenylalanine (0.057 ± 0.002, 0.055 ± 0.002, and 0.055 ± 0.004%/h for PLA, PRO, and PRO+leu, respectively; means ± SE; P = 0.850) or l-[1-13C]leucine (0.080 ± 0.004, 0.073 ± 0.004, and 0.083 ± 0.006%/h, respectively; P = 0.328). Myofibrillar l-[1-13C]phenylalanine enrichments increased following protein ingestion but did not differ between the PRO and PRO+leu treatments. In conclusion, protein ingestion before sleep improves whole body protein net balance and provides amino acids that are incorporated into myofibrillar protein during sleep. However, the ingestion of 30 g casein protein with or without additional free leucine before sleep does not increase muscle protein synthesis rates during postexercise overnight recovery.

The acute-phase protein response to human immunodeficiency virus infection in human subjects

1999 ◽  
Vol 276 (6) ◽  
pp. E1092-E1098 ◽  
Author(s):  
Farook Jahoor ◽  
Brian Gazzard ◽  
Gary Phillips ◽  
Danny Sharpstone ◽  
Melanie Delrosario ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Virus Infection ◽  
Human Immunodeficiency Virus Infection ◽  
Acute Phase ◽  
Protein Turnover ◽  
Plasma Concentrations ◽  
Retinol Binding Protein ◽  
Whole Body ◽  
Body Protein ◽  
Immunodeficiency Virus

Although several studies have shown that asymptomatic human immunodeficiency virus infection elicits an increase in whole body protein turnover, it is not known whether this increased protein turnover includes changes in the kinetics of acute-phase proteins (APPs). To answer this question, we measured 1) the plasma concentrations of four positive (C-reactive protein, α1-antitrypsin, haptoglobin, and fibrinogen) and four negative APPs [albumin, high-density lipoprotein (HDL)-apolipoprotein (apo) A1, transthyretin, and retinol-binding protein] and 2) the fractional (FSR) and absolute (ASRs) synthesis rates of three positive and three negative APPs using a constant intravenous infusion of [2H5]phenylalanine in five subjects with symptom-free acquired immunodeficiency syndrome (AIDS) and five noninfected control subjects. Compared with the values of the controls, the plasma concentrations, FSRs, and ASRs of most positive APPs were higher in the AIDS group. The negative APPs had faster FSRs in the AIDS group, there was no difference between the ASRs of the two groups, and only HDL-apoA1 had a lower plasma concentration. These results suggest that symptom-free AIDS elicits an APP response that is different from bacterial infections, as the higher concentrations and faster rates of synthesis of the positive APPs are not accompanied by lower concentrations and slower rates of synthesis of most of the negative APPs.

scholarly journals Nonessential amino acid usage for protein replenishment in humans: a method of estimation

2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Essential Amino Acids ◽  
World Health ◽  
Whole Body ◽  
Published Data ◽  
Total Proteins ◽  
Body Protein ◽  
Amino Acid Turnover

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.

Sheep of divergent genetic merit for wool growth do not differ in digesta kinetics while on restricted intakes

2014 ◽  
Vol 54 (9) ◽  
pp. 1243 ◽  
Author(s):  
I. De Barbieri ◽  
R. S. Hegarty ◽  
V. H. Oddy ◽  
M. C. Barnett ◽  
L. Li ◽  
...  
Keyword(s):  
Compartmental Model ◽  
Genetic Selection ◽  
Amino Nitrogen ◽  
Feeding Level ◽  
Wool Growth ◽  
Selection For ◽  
Fleece Weight ◽  
Estimated Breeding Values ◽  
Growth Differences ◽  
Weight Groups

Sheep selected for high wool growth were previously shown to exhibit higher microbial protein outflow from the rumen and higher uptake of amino nitrogen in portal blood than those selected for low wool growth. This suggests that genetic selection for wool growth may induce changes in foregut physiology. This study was undertaken to determine whether differences in digesta kinetics, especially mean retention mime (MRT), are associated with differences in fleece production between sheep with low or high estimated breeding values (EBVs) for fleece weight. Twenty mature Merino wethers with uniform EBVs for liveweight were allocated to two groups of 10 animals on the basis of high or low EBVs for yearling fleece weight. Five sheep with low-EBVs and five sheep with high-EBVs for fleece weight groups were allocated in a crossover design to low and high feeding-level treatments, which comprised a blended hay diet fed at maintenance or 1.5 times maintenance. All sheep were given single doses of chromium-mordanted fibre and cobalt-EDTA as inert, non-digestible markers. Digesta kinetics was determined by analysis of the faecal marker excretion patterns using a compartmental model. Higher feed intakes from animals fed 1.5 times maintenance were associated with higher rates of wool growth and higher masses of indigestible fibre in the gut, but reduced MRT of digesta. Although sheep with higher EBVs for fleece weight had higher wool growth rates, there was no indication that these wool growth differences were associated with differences in digesta kinetics. The lack of interaction between feeding level and genotype suggests that MRT did not contribute to genotype differences in wool growth in sheep fed restricted intakes. The differences in wool growth among commercial Merino sheep with divergent fleece weight EBVs achieved by multi-trait selection are not attributable to differences in digesta kinetics, at least when feed is not available ad libitum.

scholarly journals Muscle Protein Synthesis and Whole-Body Protein Turnover Responses to Ingesting Essential Amino Acids, Intact Protein, and Protein-Containing Mixed Meals with Considerations for Energy Deficit

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2457 ◽  
Author(s):  
Jess A. Gwin ◽  
David D. Church ◽  
Robert R. Wolfe ◽  
Arny A. Ferrando ◽  
Stefan M. Pasiakos
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Energy Deficit ◽  
Whole Body ◽  
Intact Protein ◽  
Body Protein ◽  
Protein Feeding

Protein intake recommendations to optimally stimulate muscle protein synthesis (MPS) are derived from dose-response studies examining the stimulatory effects of isolated intact proteins (e.g., whey, egg) on MPS in healthy individuals during energy balance. Those recommendations may not be adequate during periods of physiological stress, specifically the catabolic stress induced by energy deficit. Providing supplemental intact protein (20–25 g whey protein, 0.25–0.3 g protein/kg per meal) during strenuous military operations that elicit severe energy deficit does not stimulate MPS-associated anabolic signaling or attenuate lean mass loss. This occurs likely because a greater proportion of the dietary amino acids consumed are targeted for energy-yielding pathways, whole-body protein synthesis, and other whole-body essential amino acid (EAA)-requiring processes than the proportion targeted for MPS. Protein feeding formats that provide sufficient energy to offset whole-body energy and protein-requiring demands during energy deficit and leverage EAA content, digestion, and absorption kinetics may optimize MPS under these conditions. Understanding the effects of protein feeding format-driven alterations in EAA availability and subsequent changes in MPS and whole-body protein turnover is required to design feeding strategies that mitigate the catabolic effects of energy deficit. In this manuscript, we review the effects, advantages, disadvantages, and knowledge gaps pertaining to supplemental free-form EAA, intact protein, and protein-containing mixed meal ingestion on MPS. We discuss the fundamental role of whole-body protein balance and highlight the importance of comprehensively assessing whole-body and muscle protein kinetics when evaluating the anabolic potential of varying protein feeding formats during energy deficit.

Fibre diameter and staple strength of sheep selected for divergent clean fleece weight when subjected to an increase in intake or an increase in intake and diet change

2005 ◽  
Vol 56 (2) ◽  
pp. 195 ◽  
Author(s):  
M. A. Friend ◽  
G. E. Robards
Keyword(s):  
Growth Rate ◽  
Stepwise Regression ◽  
Fibre Diameter ◽  
Dietary Treatment ◽  
Diet Change ◽  
Wool Growth ◽  
Ad Libitum ◽  
Staple Strength ◽  
Fleece Weight ◽  
Ad Libitum Feeding

Merino wethers with a high (fleece plus, Fl+) or low (fleece minus, Fl–) potential for wool growth were offered a restricted intake of either oat grain or lucerne chaff for 8 weeks followed by ad libitum lucerne chaff for 4 weeks. The Fl– sheep that were fed oats then lucerne had a lower (P < 0.05) intake during the first 2 weeks of ad libitum feeding than all other groups. Staple strength of Fl+ sheep (37.5 ± 2.2 N/ktex) was less (P < 0.05) than that of Fl– sheep (44.5 ± 2.4 N/ktex), and dietary treatment did not significantly affect staple strength. Wool growth rate was unaffected by dietary treatment, but was greater (P < 0.001) for Fl+ (6.4 ± 0.2 µg/mm2.day) than for Fl– (4.0 ± 0.2 µg/mm2.day) sheep. Along-fibre variation in diameter was greater (P < 0.001) in Fl+ (15.6 ± 0.5%) than in Fl– (9.9 ± 0.5%) sheep. Between-fibre variation in diameter was greater (P < 0.001) in Fl+ (16.5 ± 0.5%) than in Fl– (13.2 ± 0.5%) sheep, and between-fibre variation in diameter was affected (P < 0.05) by dietary treatment in Fl+ sheep. Staple strength was significantly correlated (P < 0.05) with along-fibre variation in diameter (r = –0.48), and stepwise regression analysis indicated that along-fibre variation in diameter, wool growth rate during early restricted feeding, and minimum fibre diameter explained 63% of the variance in staple strength. The results are discussed in relation to the lower staple strength of Fl+ sheep.

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