Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Structural studies on bovine -crystallin.

Literature DB >> 5165918

Structural studies on bovine -crystallin.

Abstract

The amino acid sequences around the cysteine residues in the lens protein, gamma-crystallin, were studied. Fraction II of the gamma-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.

Entities: Chemical Species

Mesh：

Substances：

Year: 1971 PMID： 5165918 PMCID： PMC1176593 DOI： 10.1042/bj1210453

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

13 in total

Structural studies on bovine -crystallin.

1. HUMAN HEART CYTOCHROME C. CHYMOTRYPTIC PEPTIDES, TRYPTIC PEPTIDES, AND THE COMPLETE AMINO ACID SEQUENCE.

2. On the existence of an embryonic lens protein.

3. [Amino acid determination on paper chromatograms].

4. The action of trypsin on polylysine.

5. The use of thermolysin in amino acid sequence determination.

6. Studies on gamma-crystallin from calf lens. 3. Comparison of the main protein components by peptide mapping.

7. Separation of dansyl-amino acids by polyamide layer chromatography.

8. Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines.

9. A rapid and direct method for the quantitative determination of tryptophan in the intact protein.

10. Structural studies on lens proteins.

1. Isolation of a zinc protein from the tapetum lucidum of the cat.

2. The amino acid sequence of -crystallin (fraction II) from calf lens.

3. Microheterogeneity at the C-terminus of gamma-crystallin fraction IVb.

4. C-terminal amino acid sequence of bovine -crystallin.

5. Modification of calf lens crystallins as determined by gel electrophoresis.