scholarly journals Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39

1974 ◽  
Vol 143 (1) ◽  
pp. 233-240 ◽  
Author(s):  
Jean-Marie Frère ◽  
Ramon Moreno ◽  
Jean-Marie Ghuysen ◽  
Harold R. Perkins ◽  
Louis Dierickx ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain

The exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase–transpeptidase from Streptomyces R61.

scholarly journals Molecular weight and amino acid composition of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61

1973 ◽  
Vol 135 (3) ◽  
pp. 463-468 ◽  
Author(s):  
J.-M. Frère ◽  
J.-M. Ghuysen ◽  
H. R. Perkins ◽  
M. Nieto
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain

A procedure allowing the purification of milligram amounts of the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R61 to protein homogeneity (95% purity) is described. The isolated protein has a molecular weight of about 38000 and consists of one polypeptide chain. Its amino acid composition is presented.

The isolation and properties of 1·6 S γ -histone from calf thymocytes

1958 ◽  
Vol 149 (934) ◽  
pp. 36-41 ◽  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
High Molecular Weight ◽  
Acid Composition ◽  
The Other ◽  
Amino Acid Compositions

The isolation of 1·6 S γ -histone is described, its amino-acid composition recorded and an account given of some of its physicochemical properties. Its molecular weight has been calculated from sedimentation velocities to be 74000 in its unaggregated condition. It thus represents a second histone of high molecular weight present in the nuclei of calf thymocytes. Both β and 1·6 S γ -histone are distinguished from the other four components in their ability to undergo aggregation. The γ -histone, however, does not aggregate so readily or so extensively as does β -histone. These two histones are also clearly distinguished by their amino-acid compositions.

scholarly journals  Quality of rabbit meat and phyto-additives

2010 ◽  
Vol 28 (No. 3) ◽  
pp. 161-167 ◽  
Author(s):  
M.P. Simonová ◽  
Ľ. Chrastinová ◽  
J. Mojto ◽  
A. Lauková ◽  
R. Szábová ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Plant Extracts ◽  
Good Health ◽  
Good Alternative ◽  
Health State ◽  
Rabbit Meat

The consumption of healthy and nutritive food (rich in proteins and low in cholesterol and lipid contents) is a preferred factor with the contemporary consumers. In addition, natural alternatives are requested to replace the additives used up to now but recently banned. To reach the above given condition, phyto-additives represent a good alternative. The aim of this study was to examine the physicochemical properties and amino acid composition of rabbit meat after the enrichment of rabbit diet with oregano, sage, and Eleutherococcus senticosus extracts, and to make a comparison with the commercial product XTRACT and control samples (without plant extracts). The addition of oregano and sage extracts as well as El. senticosus in the rabbit diet positively influenced the physicochemical properties of rabbit meat by increasing its energy value (P < 0.05 – sage). Supplementing rabbits feed with oregano and sage extracts led to an improvement on the amino acid composition (P < 0.01; P < 0.001 – serine). These findings are also supported by the good health state of rabbits. Outgoing from these results, the diet enriched with the plant extracts is beneficial for the health state of rabbits involving the nutritional quality of rabbit meat in connection with consumers.

Amino acid composition and molecular weight of Botrytis cinerea laccase

1977 ◽  
Vol 16 (7) ◽  
pp. 1051-1052 ◽  
Author(s):  
Alfred M. Mayer ◽  
Irith Marbach ◽  
Assa Marbach ◽  
Ada Sharon
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Botrytis Cinerea ◽  
Acid Composition

scholarly journals Separation and partial characterization of guinea-pig caseins

1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Exchange Chromatography

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.

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