Effect of Ascorbic Acid on Guinea Pig Skin Collagen Synthesis: II. Neutral and Acid Soluble Collagens, Mucopolysaccharides, and Amino Acid Composition

1969 ◽  
Vol 48 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Virginia Richmond ◽  
E.L.R. Stokstad
Keyword(s):  
Ascorbic Acid ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Collagen Synthesis ◽  
Pig Skin ◽  
Skin Collagen

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.

SOME PROPERTIES OF APOFERRITIN ISOLATED FROM GUINEA PIG LIVER

1962 ◽  
Vol 40 (1) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Guinea Pigs ◽  
Dicarboxylic Acids ◽  
Acetate Buffer ◽  
Pig Liver ◽  
Guinea Pig Liver

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.

scholarly journals Importance of amino acid composition to improve skin collagen protein synthesis rates in UV-irradiated mice

Amino Acids ◽  
2011 ◽  
Vol 42 (6) ◽  
pp. 2481-2489 ◽  
Author(s):  
Hitoshi Murakami ◽  
Kazutaka Shimbo ◽  
Yoshiko Inoue ◽  
Yoshinobu Takino ◽  
Hisamine Kobayashi
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Collagen Protein ◽  
Skin Collagen

scholarly journals The products from papain and pepsin hydrolyses of guinea-pig immunoglobulins γ1G and γ2G

1971 ◽  
Vol 121 (5) ◽  
pp. 829-837 ◽  
Author(s):  
R G Q Leslie ◽  
M. D. Melamed ◽  
S. Cohen
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Antigenic Specificity ◽  
Antigenic Properties ◽  
Peptic Digestion ◽  
A Site ◽  
Papain Digestion

1. The products from papain and pepsin hydrolyses of the guinea-pig immunoglobulins γ1G and γ2G were isolated and characterized with regard to molecular weight, amino acid composition, hexose content and antigenic specificity. 2. Fragments Fab and (Fab′)2 from immunoglobulins γ1G and γ2G have similar electrophoretic and antigenic properties, but show some class-specific differences in amino acid composition. 3. Three Fc fragments were obtained after papain digestion of immunoglobulin γ2G, namely, fragment Fc dimer (mol.wt. 58000), fragment Fc monomer (mol.wt. 29000) and fragment Fc′ (mol.wt. 8000). A single crystalline fragment, namely fragment Fc′ (mol.wt. 11000), was isolated after papain digestion of immunoglobulin γ1G. 4. Peptic digestion of immunoglobulins γ1G and γ2G releases C-terminal fragments, namely, fragments pFc′, of similar molecular weight (13000) but different amino acid compositions and distinct antigenic specificities. 5. Digestion-time studies show that immunoglobulin γ1G is far more susceptible to proteolysis than is immunoglobulin γ2G and suggest that at least a proportion of molecules are split primarily at a site that liberates fragment γ1Fc′.

SOME PROPERTIES OF APOFERRITIN ISOLATED FROM GUINEA PIG LIVER

1962 ◽  
Vol 40 (8) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Guinea Pigs ◽  
Dicarboxylic Acids ◽  
Acetate Buffer ◽  
Pig Liver ◽  
Guinea Pig Liver

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.

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