Solving the woolly mammoth conundrum: amino acid 15N-enrichment suggests a distinct forage or habitat

Nodules of certain N2-fixing root nodules are substantially enriched in 15N compared with non-nodular tissues. This enrichment usually resides largely within bacteroids. Isotope discrimination associated with export of ammonia(um) from the bacteroid would result in 15N enrichment of NH4+ within bac- teroids. Bacteroid protein synthesis from this pool of 15N enriched NH4+ would then account for enrichment of the bacteroids. Measurements of 15N abundances of total N and free NH4+ in nodule fractions from lupins (Lupinus luteus), soybeans (Glycine max) and peas (Pisum sativum) showed this was not the case. With the inocula used in experiments reported here, lupin and soybean nodules were enriched in 15N, while pea nodules were not. There was no correlation between 15N abundances of NH4+ and total N in the nodule fractions (r= 0.445, P> 0.2). We conclude that isotope discrimination associated with ammonia(um) transport does not explain the 15N elevation of lupin and soybean nodules. We also conclude, on the basis of the large isotope effect for the equilibrium between NH4+ and NH3, that most of the ammonia(um) is exported from bacteroids as NH4+ rather than NH3. We also measured the 15N abundance of free amide N. There was a strong correlation between 15N abundances of free amide N and total N in nodule fractions (r=0.924, P<0,001), suggesting that amide N is a significant source of N to the amino acid pools from which proteins are synthesised.

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Roles of Amino Acid Residues in Woolly Mammoth Hemoglobin on the Temperature Effect of Oxygen Binding

Biophysical Journal ◽

10.1016/j.bpj.2012.11.3099 ◽

2013 ◽

Vol 104 (2) ◽

pp. 559a

Author(s):

Yue Yuan ◽

Catherine Byrd ◽

Tong-Jian Shen ◽

Nancy T. Ho ◽

Virgil Simplaceanu ◽

...

Keyword(s):

Amino Acid ◽

Temperature Effect ◽

Oxygen Binding ◽

Amino Acid Residues ◽

Effect Of Oxygen ◽

Woolly Mammoth

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Real Ileal Digestibility of Sunflower Protein and Amino Acids in Humans

Current Developments in Nutrition ◽

10.1093/cdn/nzaa049_060 ◽

2020 ◽

Vol 4 (Supplement_2) ◽

pp. 667-667

Author(s):

Romain Tessier ◽

Juliane Calvez ◽

Nadezda Khodorova ◽

Alain Quinsac ◽

Romain Kapel ◽

...

Keyword(s):

Amino Acid ◽

Protein Isolate ◽

National Agency ◽

Ileal Digestibility ◽

Dietary Nitrogen ◽

Healthy Humans ◽

Indispensable Amino Acid ◽

15N Enrichment ◽

Sunflower Protein ◽

Exogenous Nitrogen

Abstract Objectives Sunflower protein has a relatively well-balanced amino acid profile but it is little used in human food. Nutritional quality of sunflower protein isolate has never been directly measured in humans. This study aims to determine the ileal digestibility of protein and amino acid of a sunflower isolate incorporated in biscuits, in healthy humans. Methods Healthy volunteers (n = 7) were intubated with a naso-ileal tube. They ingested every 30 min for 4 h, sunflower biscuits for a total of 156 g of biscuits and 25 g of 15N intrinsically labeled sunflower protein isolate. A non-absorbable marker was perfused into the ileum. Ileal samples were continuously collected during 8 h after the first meal. Blood was sampled every 30 min for 4 h and every hour after and total urine was collected every 2 h. To measure nitrogen ileal digestibility, the percentage of nitrogen and 15N enrichment in ileal contents were assessed by an elemental analyzer coupled with and isotope ratio mass spectrometer (EA-IRMS). Indispensable amino acid (IAA) ileal digestibility was determined by measuring amino acid 15N enrichment by GC-C-IRMS and their quantification by UHPLC. Metabolic losses of dietary nitrogen were assessed by measuring 15N in urine and plasma. The digestible indispensable amino acid score (DIAAS) and the net post-prandial utilization (NPPU) were calculated. Results Exogenous nitrogen appeared in the ileum 1 h after the first meal, its flow was stable between 4 h and 7 h. Cumulated dietary nitrogen in the ileum was 14.0 ± 4.0% over 8 h. Sunflower nitrogen real ileal digestibility was 86.0 ± 4.0% of ingested nitrogen. Mean IAA ileal digestibility was 87.0 ± 6.1% with values ranging from 84.4% for lysine and threonine to 89.3 ± 7.8% for methionine. DIAAS was 0.93 for lysine. After 8 h, 4.0 ± 1.0% of dietary nitrogen was incorporated in plasma protein. Cumulated exogenous nitrogen in urinary urea was 4.0 ± 1.4% and exogenous nitrogen in body urea after 8 h was 9.8 ± 2.5%. The NPPU was 72.2 ± 3.7% at 8 h. Conclusions Sunflower isolate ileal digestibility is relatively low compared to other protein isolate assessed in similar conditions (ileal tube and 15N labeling of protein). Despite a moderate deficiency in lysine, sunflower protein isolate has a good post-prandial metabolic utilization. Funding Sources French Research National Agency (ANR), financial support of SOFIPROTEOL under the FASO Project PRODIA.

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Effects of early amino acid administration during total parenteral nutrition on protein metabolism in pre-term infants

Clinical Science ◽

10.1042/cs0820199 ◽

1992 ◽

Vol 82 (2) ◽

pp. 199-203 ◽

Cited By ~ 90

Author(s):

R. A. van Lingen ◽

J. B. van Goudoever ◽

I. H. T. Luijendijk ◽

J. L. D. Wattimena ◽

P. J. J. Sauer

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Birth Weight ◽

Amino Acid ◽

Protein Breakdown ◽

Protein Balance ◽

15N Enrichment ◽

Group A ◽

Group B ◽

Acid Administration

1. We investigated the effects of starting amino acid administration on post-natal day 2 on protein turnover and nitrogen balance in appropriate-for-gestational-age, very-low-birth-weight infants. Eighteen infants were divided into two groups. Group A received from day 2 onwards an amino acid solution, whereas group B started on this solution after day 4. Both groups were exclusively parenterally fed, 200 kJ day−1 kg−1 on post-natal days 3 and 4. Group A (birth weight 1.5 ± 0.3 kg) received 4.6 g of glucose, 1.9 g of fat and 2.3 g of amino acids day−1 kg−1 body weight. Group B (birth weight 1.4 ± 0.2 kg) received 7.0 g of glucose and 1.9 g of fat day−1 kg−1 body weight. 2. At post-natal day 3, a primed constant infusion of 3 mg of [15N]glycine day−1 kg−1 was given. Protein flux, protein synthesis and protein breakdown were calculated from the 15N enrichment in urinary ammonia. In five out of nine infants in group B no plateau of 15N enrichment in urinary urea could be detected, whereas in group A two out of nine infants did not reach a plateau. For this reason we did not use the end product urea for our calculations. 3. The administration of the amino acids resulted in a higher protein flux (6.9 ± 1.5 g day−1 kg−1 versus 5.2 ± 0.9 g day−1 kg−1) and a higher protein synthesis rate (6.0 ± 1.4 g day−1 kg−1 versus 4.6 ± 0.8 g day−1 kg−1) in group A. There was no statistically significant difference in protein breakdown. The administration of amino acids reversed a negative protein balance (−0.6 ± 0.2 g day−1 kg−1) into a positive one (1.4 ± 0.2 g day−1 kg−1. No adverse effects of the amino acid infusion were seen. 4. We conclude that the early introduction of amino acids has, even at this relatively low energy intake of 200 kJ day−1 kg−1, a positive effect on protein balance by increasing protein synthesis.

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Elephantid genomes reveal the molecular bases of Woolly Mammoth adaptations to the arctic

10.1101/018366 ◽

2015 ◽

Cited By ~ 1

Author(s):

Vincent Lynch ◽

Oscar C. Bedoya-Reina ◽

Aakrosh Ratan ◽

Michael Sulak ◽

Daniela I. Drautz-Moses ◽

...

Keyword(s):

Amino Acid ◽

Transient Receptor Potential ◽

Thermal Sensation ◽

Nuclear Genome ◽

Receptor Potential ◽

The Arctic ◽

Temperature Sensitive ◽

Genetic Changes ◽

Specific Amino Acid ◽

Woolly Mammoth

Woolly mammoths and the living elephants are characterized by major phenotypic differences that allowed them to live in very different environments. To identify the genetic changes that underlie the suite of adaptations in woolly mammoths to life in extreme cold, we sequenced the nuclear genome from three Asian elephants and two woolly mammoths, identified and functionally annotated genetic changes unique to the woolly mammoth lineage. We find that genes with mammoth specific amino acid changes are enriched in functions related to circadian biology, skin and hair development and physiology, lipid metabolism, adipose development and physiology, and temperature sensation. Finally we resurrect and functionally test the mammoth and ancestral elephant TRPV3 gene, which encodes a temperature sensitive transient receptor potential (thermoTRP) channel involved in thermal sensation and hair growth, and show that a single mammoth-specific amino acid substitution in an otherwise highly conserved region of the TRPV3 channel strongly affected its temperature sensitivity. Our results have identified a set of genetic changes that likely played important roles in the adaptation of woolly mammoths to life in the high artic.

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The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142372 ◽

1986 ◽

Vol 44 ◽

pp. 150-151

Author(s):

M.K. Lamvik ◽

L.L. Klatt

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Staining Pattern ◽

Banding Patterns ◽

Mass Thickness ◽

New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

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Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142311 ◽

1986 ◽

Vol 44 ◽

pp. 134-135

Author(s):

A. J. Tousimis

Keyword(s):

Small Intestine ◽

Amino Acid ◽

Epithelial Cells ◽

Elemental Composition ◽

Isotope Labeling ◽

Structural Components ◽

X Ray ◽

Human Small Intestine ◽

Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

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Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100147776 ◽

1993 ◽

Vol 51 ◽

pp. 388-389

Author(s):

Chi-Ming Wei ◽

Margaret Hukee ◽

Christopher G.A. McGregor ◽

John C. Burnett

Keyword(s):

Amino Acid ◽

Natriuretic Peptide ◽

Vascular Tone ◽

Cardiac Tissue ◽

Ring Structure ◽

Terminal Amino Acid ◽

Amino Acid Peptide ◽

Normal Human ◽

Terminal Amino ◽

The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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