Amino acid composition of skeletal muscle of domestic buffalo (Bos bubalus L.)—I. Comparative studies and nutritional value of proteins

Author(s):  
Letizia Cutinelli-Ambesi ◽  
Vincenzo Bocchini ◽  
Ciro Balestrieri ◽  
Francesco Salvatore
1992 ◽  
Vol 40 (1) ◽  
pp. 98-106
Author(s):  
Constantinos G. Zarkadas ◽  
Elizabeth. Larmond ◽  
James I. Elliot ◽  
Ali D. Khalili ◽  
Carol. Beddard-Neil

2018 ◽  
Vol 8 (1) ◽  
pp. 637-643
Author(s):  
T.L. Holubenko

<p><span lang="EN-US">The aim of the research is to assess the amino acid composition of veal from different genotype bull-calves concerning the usage in baby food production. A comparative analysis of the essential amino acids content in meat of calves of <span>black-and-white motley breed,</span> Aberdeen Angus breed and black and white crossbreeds grown according to the traditional technology of dairy cattle breeding hasn’t showed any significant differences. However, some differences were observed for each separate amino acid. Although the difference in amino acids was 2. 9% in favor of <span>black-and-white motley breed</span>. According to the amino acid composition, the calves meat of Charolais breed is biologically more complete than the Aberdeen Angus calves meat of the first generation in the valine content by 7.4%, isoleucine by 45.3% (P &lt;0.001), leucine by 15.2% (P &lt;0.001), lysine by 7.8%, threonine and phenylalanine + tyrosine by 6.5% (P &lt;0.05) and 7.5% (P &lt;0.01), respectively. Amino acid content was limited by the sum of amino acids phenylalanine + tyrosine (80.2%) in purebreds and methionine + cystine (83.4%) in <span>crossbreeds</span>. The other amino acids content was more than 100%; it indicates a high biological and nutritional value of veal. In the first experiment, the degree of compliance with the norms of a balanced diet is 37.4-38.2%. The human body's need for such essential amino acids as valine, isoleucine, phenylalanine + tyrosine is satisfied for more than 20%; the human body's need for leucine, lysine, and threoni9ne is satisfied for more than 30%. Veal of the Charolaise young is distinguished by higher indicators. The degree of its compliance with the norms of a balanced diet is 43.8% against 37.6% in hybrid calves. It is proved that veal obtained from young animals of different breeds in ecologically clean zones has a high biological and nutritional value, it corresponds to the indices for meat raw materials for baby food in accordance with Sanitary Norms 11-63 RB98.</span></p>


1997 ◽  
Vol 326 (3) ◽  
pp. 641-648 ◽  
Author(s):  
Maria RANIERI-RAGGI ◽  
Umberto MONTALI ◽  
Francesca RONCA ◽  
Antonietta SABBATINI ◽  
Paul E. BROWN ◽  
...  

Denaturation of rabbit skeletal-muscle AMP deaminase in acidic medium followed by chromatography on DEAE-cellulose in 8 M urea at pH 8.0 allows separation of two main peptide components of similar apparent molecular mass (75–80 kDa) that we tentatively assume correspond to two different enzyme subunits. Whereas the amino acid composition of one of the two peptides is in good agreement with that derived from the nucleotide sequence of the known rat and human AMPD1 cDNAs, the second component shows much higher contents of proline, glycine and histidine. N-Terminal sequence analysis of the fragments liberated by limited proteolysis with trypsin of the novel peptide reveals a striking similarity to the fragments produced by plasmin cleavage of the rabbit plasma protein called histidine–proline-rich glycoprotein (HPRG). However, some divergence is observed between the sequence of one of the fragments liberated from AMP deaminase by a more extensive trypsinization and rabbit plasma HPRG in the region containing residues 472–477. A fragment with a blocked N-terminus, which was found among those liberated by proteolysis with pepsin of either whole AMP deaminase or the novel component of the enzyme, shows an amino acid composition quite different from that of the N-terminus of the known subunit of AMP deaminase. By coupling this observation with the detection in freshly prepared AMP deaminase of a low yield of the sequence (LTPTDX) corresponding to that of HPRG N-terminus, it can be deduced that in comparison with HPRG, the putative HPRG-like component of AMP deaminase contains an additional fragment with a blocked N-terminus, which is liberated by a proteolytic process during purification of the enzyme. The implications of the association to rabbit skeletal-muscle AMP deaminase of a HPRG-like protein species are discussed.


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