Molecular weight and amino acid composition of five-times-crystallized phosphoglucose isomerase from rabbit skeletal muscle

Biochemistry ◽  
1970 ◽  
Vol 9 (7) ◽  
pp. 1506-1514 ◽  
Author(s):  
Ning G. Pon ◽  
Klaus D. Schnackerz ◽  
Michael N. Blackburn ◽  
Gora C. Chatterjee ◽  
Ernst A. Noltmann
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Phosphoglucose Isomerase ◽  
Rabbit Skeletal Muscle

scholarly journals Association of purified skeletal-muscle AMP deaminase with a histidine–proline-rich-glycoprotein-like molecule

1997 ◽  
Vol 326 (3) ◽  
pp. 641-648 ◽  
Author(s):  
Maria RANIERI-RAGGI ◽  
Umberto MONTALI ◽  
Francesca RONCA ◽  
Antonietta SABBATINI ◽  
Paul E. BROWN ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Rabbit Skeletal Muscle ◽  
Striking Similarity ◽  
The Novel ◽  
Amp Deaminase ◽  
Rabbit Plasma ◽  
N Terminus

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.

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.

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