Use of protected amino acids to increase duodenal amino acid supply in lactating dairy cows

1990 ◽  
Vol 1990 ◽  
pp. 18-18
Author(s):  
D E Beever ◽  
D J Napper ◽  
B Sloan
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Dairy Cows ◽  
Ph Sensitive ◽  
Rumen Degradation ◽  
Lactating Dairy Cows ◽  
Ph Sensitive Polymer ◽  
In Vivo Assessment

Augmenting the supply of specific amino acids to pigs and poultry is straightforward cbinpared with ruminants where fermentation in the forestomach may reduce the proportion of the supplement which ultimately reaches the small intestine. Recently there have been several attempts to develop amino acid supplements which escape rumen degradation, thus optimising the increase in duodenal amino acid supply. The work reported in this study provides an in vivo assessment of one such product - namely lysine and methionine coated with a pH sensitive polymer.

scholarly journals Harnessing the value of rumen protected amino acids to enhance animal performance

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Mitra Mazinani ◽  
Erdogan Memili ◽  
Brian J. Rude
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Current Trend ◽  
Building Blocks ◽  
Microbial Protein ◽  
Daily Production ◽  
Main Site ◽  
Rumen Degradation ◽  
Amino Acid Requirements

Abstract In general, higher mammals need nine amino acids in their diets as building blocks to synthesize proteins while ruminants can produce some of them through the synthesis of microbial proteins. Diet is utilized by ruminal microorganisms to synthesize microbial protein (MCP) which is digested in the small intestine (SI). Although protein and amino acid requirements in ruminants are subject to microbial protein synthesis, it is not enough for optimal daily production. Therefore, there is a current trend towards supplementing amino acids in ruminant diets. In the rumen, free amino acids can be degraded by rumen bacteria, therefore, the AAs need to be supplemented in a protected form to be stable in the rumen and absorbable post-ruminal for metabolic purposes. The main site of amino acid absorption is the small intestine (SI), and there is a need to keep AA from ruminal degradation and direct them to absorption sites. Several approaches have been suggested by feed scientists to decrease this problem such as defaunation and debacterization of the rumen against amino acid-fermenting fungi and bacteria, inhibitors or antagonists of vitamin B6 enzymes, diet composition and also protecting AA from rumen degradation. A number of studies have evaluated the roles of amino acids concerning their effects on milk yield, growth, digestibility, feed intake and efficiency of nitrogen utilization of ruminants. The focus of this review was on experimental and research studies about AAs in feedstuff, metabolism, supplementing amino acids for ruminants and the current trends of using rumen protected amino acids.

The influence of the method of preservation of forages on the digestion in dairy cows. 2. Digestion of organic matter, energy and amino acids in forestomachs and intestines.

1975 ◽  
Vol 23 (2) ◽  
pp. 89-103
Author(s):  
S. Tamminga
Keyword(s):  
Amino Acids ◽  
Organic Matter ◽  
Small Intestine ◽  
Amino Acid ◽  
Formic Acid ◽  
Dairy Cows ◽  
Grass Silage ◽  
Matter Energy

2. Two dairy cows with duodenal reentrant and rumen cannulae were given diets containing artificially dried and pelleted grass (GP), grass silage treated with formic acid (GSF), grass silage treated with a mixture of formic acid and formaldehyde (GSFF) or grass silage without additive (GS). DM intake was 14.8 to 16.0 kg/day and about 30% of the N in the diets was from grass pellets or silages. Between 45 and 57% of the apparently digested organic matter and between 26 and 41% of the apparently digested energy disappeared before the intestines. The higher values were found with GSF and GS.Total amino acid N reaching the duodenum was between 104 and 134% of intake, highest with GP and GSFF. The amounts of individual amino acids reaching the small intestine were from 75 to 270% of the amounts ingested. High values (>150%) were found for glycine, lysine, methionine and tyrosine; low values (

scholarly journals Postruminal Delivery System for Amino Acids and Proteins in Cattle

2007 ◽  
Vol 76 (4) ◽  
pp. 547-552 ◽  
Author(s):  
T. Sýkora ◽  
M. Rabišková ◽  
J. Třináctý ◽  
D. Vetchý ◽  
A. Häring ◽  
...  
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Low Cost ◽  
Ph Sensitive ◽  
Wet Granulation ◽  
Average Weight ◽  
Disintegration Time ◽  
The Core ◽  
Ph Sensitive Polymer

The purpose of this experiment was to develop an effective postruminal transport system (PTS) with a high content of suitable vegetable proteins and amino acids. PTS serves for nutrient delivery to the abomasum and small intestine of dairy cows in order to increase the milk yield. Direct addition of proteins and amino acids to the diet is not useful as the ruminal microbes will utilize active substances before they reach absorption sites in the small intestine. PTS has several advantages, e.g. a possibility of the direct application in a food, low cost, and nutritional and therapeutical improvement. PTS consists of a core (pellets, small tablets) and a coating, which protects the core against the environment of rumen and enables to release the core content in the environment of abomasum and small intestine. Lenticular tablets - cores of PTS were prepared by wet granulation method and compression. Qualitative indicators of tablets (average weight, weight uniformity, hardness, friability, disintegration time) were determined according to valid Czech and European Pharmacopoeias. Cores were subsequently coated with several types of coating - ethylcellulose, stearic acid and pH sensitive polymer poly-(2-vinylpyridine-co-styren), alone or in combination of various rates. Nine samples of coated protein tablets exhibiting appropriate characteristics in vitro were prepared. The presence of the pH sensitive polymer at least in 10% concentration of the coating and the coating amount of 9.0 to 12.6% per tablet were necessary to ensure the requested PTS properties.

Comparison and evaluation of protein evaluation systems currently in use in europe

1993 ◽  
Vol 1993 ◽  
pp. 6-6
Author(s):  
W.M. van Straalen ◽  
C. Salaün
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Evaluation Systems ◽  
Rumen Degradation ◽  
Small Intestinal ◽  
Feed Protein ◽  
True Protein

In modern protein evaluation systems the protein unit (PU) of a feedstuff and the requirement of PU is expressed as true protein assumed to be absorbed from the small intestine. Total PU supply originates from feed protein escaping rumen degradation and from microbial protein synthesised in the rumen. Escape feed PU is calculated from crude protein (CP) multiplied by the escape CP fraction, amino acid content of escape CP and small intestinal digestibility of escape amino acids. Microbial PU is calculated from the energy source for microbial growth multiplied by the efficiency by which this energy is used for microbial CP synthesis, amino acid content of microbial CP and the digestibility in the small intestine of microbial amino acids.

On the Role of Branched-Chain Amino Acids in Protein Turnover of Skeletal Muscle. Studies in vivo with L-Norleucine

1985 ◽  
Vol 40 (5-6) ◽  
pp. 427-437 ◽  
Author(s):  
Klaus-Joachim Schott ◽  
Jochen Gehrmann ◽  
Ulla Potter ◽  
Volker Neuhoff
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Small Intestine ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Protein Concentration ◽  
Amino Acid Concentrations

Abstract 1. The effect of ʟ-norleucine, an isomer of leucine, on protein metabolism in vivo was studied in suckling rats. Rats were injected subcutaneously with various doses of ʟ-norleucine (0.5 and 5.0 μmol/g body wt.) every 12 h from 3 to 15 days post partum. Protein concentration, amino acid concentrations, and incorporation of [3H]tyrosine into protein were analyzed in liver, muscles of thigh and small intestine. Amino acid concentrations and insulin levels in serum were also measured. 2. At 5 days of age, norleucine induced an increase in protein concentration of skeletal muscle with an increased incorporation of [3H]tyrosine into protein indicating an accelerated protein synthesis. Changes in protein metabolism were paralleled by alterations in the amino acid pattern of this tissue. 3. When protein concentration and protein synthesis were increased in skeletal muscle, protein concentration of small intestine was decreased, accompanied by elevated levels of amino acids in tissue. Protein synthesis of small intestine was not altered by the norleucine treatment. The results suggest a close interrelationship between skeletal muscle and small intestine with respect to protein turnover. 4. The effects of norleucine were less pronounced at 10 and 15 days of age, which indicates a metabolic adaptation to the treatment. 5. Alterations in amino acid concentrations of tissue due to changes in protein metabolism were not uniform but tissue-specific. 6. Current concepts for explaining the effects of branched-chain amino acids (BCAA) on protein turnover in skeletal muscle are based on the assumption that the BCAA or leucine alone might become rate-limiting for protein synthesis in muscle under catabolic conditions. The amino acid analogue norleucine, however, cannot replace any of the BCAA in protein. Additionally, norleucine affected protein metabolism in highly anabolic organisms. Therefore, the present thoughts on this issue appear to be incomplete.

scholarly journals Primary structure requirements for correct sorting of the yeast mitochondrial protein ADH III to the yeast mitochondrial matrix space.

1987 ◽  
Vol 7 (1) ◽  
pp. 294-304 ◽  
Author(s):  
D Pilgrim ◽  
E T Young
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Amino Acid ◽  
Proteolytic Processing ◽  
Mitochondrial Matrix ◽  
Wild Type ◽  
Mature Form ◽  
Amino Terminal ◽  
The Matrix

Alcohol dehydrogenase isoenzyme III (ADH III) in Saccharomyces cerevisiae, the product of the ADH3 gene, is located in the mitochondrial matrix. The ADH III protein was synthesized as a larger precursor in vitro when the gene was transcribed with the SP6 promoter and translated with a reticulocyte lysate. A precursor of the same size was detected when radioactively pulse-labeled proteins were immunoprecipitated with anti-ADH antibody. This precursor was rapidly processed to the mature form in vivo with a half-time of less than 3 min. The processing was blocked if the mitochondria were uncoupled with carbonyl cyanide m-chlorophenylhydrazone. Mutant enzymes in which only the amino-terminal 14 or 16 amino acids of the presequence were retained were correctly targeted and imported into the matrix. A mutant enzyme that was missing the amino-terminal 17 amino acids of the presequence produced an active enzyme, but the majority of the enzyme activity remained in the cytoplasmic compartment on cellular fractionation. Random amino acid changes were produced in the wild-type presequence by bisulfite mutagenesis of the ADH3 gene. The resulting ADH III protein was targeted to the mitochondria and imported into the matrix in all of the mutants tested, as judged by enzyme activity. Mutants containing amino acid changes in the carboxyl-proximal half of the ADH3 presequence were imported and processed to the mature form at a slower rate than the wild type, as judged by pulse-chase studies in vivo. The unprocessed precursor appeared to be unstable in vivo. It was concluded that only a small portion of the presequence contains the necessary information for correct targeting and import. Furthermore, the information for correct proteolytic processing of the presequence appears to be distinct from the targeting information and may involve secondary structure information in the presequence.

scholarly journals BIOSYNTHESIS IN ISOLATED ACETABULARIA CHLOROPLASTS

1972 ◽  
Vol 54 (2) ◽  
pp. 279-294 ◽  
Author(s):  
David C. Shephard ◽  
Wendy B. Levin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Technical Problems ◽  
Hydrolyzed Protein ◽  
Protein Amino Acids ◽  
Amino Acid Labeling ◽  
Labeling Pattern

The ability of chloroplasts isolated from Acetabulana mediterranea to synthesize the protein amino acids has been investigated. When this chloroplast isolate was presented with 14CO2 for periods of 6–8 hr, tracer was found in essentially all amino acid species of their hydrolyzed protein Phenylalanine labeling was not detected, probably due to technical problems, and hydroxyproline labeling was not tested for The incorporation of 14CO2 into the amino acids is driven by light and, as indicated by the amount of radioactivity lost during ninhydrin decarboxylation on the chromatograms, the amino acids appear to be uniformly labeled. The amino acid labeling pattern of the isolate is similar to that found in plastids labeled with 14CO2 in vivo. The chloroplast isolate did not utilize detectable amounts of externally supplied amino acids in light or, with added adenosine triphosphate (ATP), in darkness. It is concluded that these chloroplasts are a tight cytoplasmic compartment that is independent in supplying the amino acids used for its own protein synthesis. These results are discussed in terms of the role of contaminants in the observed synthesis, the "normalcy" of Acetabularia chloroplasts, the synthetic pathways for amino acids in plastids, and the implications of these observations for cell compartmentation and chloroplast autonomy.

scholarly journals Regulation of rat magnocellular neurosecretory system by D-aspartate: evidence for biological role(s) of a naturally occurring free D-amino acid in mammals

2000 ◽  
Vol 167 (2) ◽  
pp. 247-252 ◽  
Author(s):  
H Wang ◽  
H Wolosker ◽  
J Pevsner ◽  
SH Snyder ◽  
DJ Selkoe
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Amino Acid ◽  
Physiological Function ◽  
Neurosecretory System ◽  
Milk Ejection ◽  
Magnocellular Neurons ◽  
Rat Hypothalamus ◽  
Naturally Occurring

Little evidence is available for the physiological function of D-amino acids in species other than bacteria. Here we demonstrate that naturally occurring freed -aspartate (D-Asp) is present in all magnocellular neurons of rat hypothalamus. The levels of this naturally occurring D-amino acid were elevated during lactation and returned to normal thereafter in the magnocellular neurosecretory system, which produces oxytocin, a hormone responsible for milk ejection during lactation. Intraperitoneal injections of D-Asp reproducibly increased oxytocin gene expression and decreased the concentration of circulating oxytocin in vivo. Similar changes were observed in the vasopressin system. These results provide evidence for the role(s) of naturally occurring free D-Asp in mammalian physiology. The findings argue against the conventional concept that only L-stereoisomers of amino acids are functional in higher species.

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