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.

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.

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.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

Acid Proteases From Species of Mucor: Molecular Weight of Mucor miehei Protease From Amino Acid Analysis Data

1973 ◽  
Vol 51 (12) ◽  
pp. 1638-1646 ◽  
Author(s):  
W. S. Rickert ◽  
J. R. Elliott
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Weight Function ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Analysis ◽  
Analysis Data ◽  
Improved Method ◽  
Mucor Miehei ◽  
A Value

An improved method for the isolation of Mucor miehei protease which utilizes a diafiltration cell has been used to obtain a highly purified protein in gram quantities and yields of about 80%. Based on a modified molecular weight function and data from amino acid analysis, a value of 41 800 for the molecular weight of the glycoprotein was established and some modification to the published amino acid composition was made. These results suggest that Mucor miehei protease is distinctly different from the two other acid proteases which are also produced by species of Mucor.

Molecular weight and amino acid composition of purified spinach beet phenolase

1975 ◽  
Vol 14 (11) ◽  
pp. 2383-2386 ◽  
Author(s):  
P.F.T. Vaughan ◽  
R. Eason ◽  
J.Y. Paton ◽  
G.A. Ritchie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition
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