COVALENT STRUCTURE OF CALF SKIN TYPE-III COLLAGEN .4. AMINO-ACID SEQUENCE OF THE CYANOGEN-BROMIDE PEPTIDE ALPHA-1(III)CB5 (POSITIONS 552-788)
- 1 January 1979
- journal article
- research article
- Vol. 360 (7), 841-850
Abstract
The CNBr peptide .alpha.1(III)CB5 is 237 amino acid residues in length and occupies position 552-788 along the .alpha.1(III) chain. For sequence analysis .alpha.1(III)CB5 was fragmented with hydroxylamine, protease from Staphylococcus aureus V8, trypsin [EC 3.4.21.4] and the arginine-specific enzyme from mouse submaxillary gland. The peptides obtained were separated using molecular and ion exchange chromatography and sequenced with the automated Edman degradation procedure.This publication has 4 references indexed in Scilit:
- COVALENT STRUCTURE OF CALF SKIN TYPE-III COLLAGEN .5. AMINO-ACID SEQUENCE OF THE CYANOGEN-BROMIDE PEPTIDE ALPHA-1(III)CB9A (POSITION 789 TO 927)1979
- HEMOGLOBINS .21. SEQUENCE-ANALYSIS OF PORCINE HEMOGLOBIN1978
- Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liverBiochemistry, 1977
- Isolation and Characterization of CNBr Derived Peptides of the α1 (III) Chain of Pepsin-Solubilized Calf Skin CollagenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976