Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liver

Biochemistry ◽  
1977 ◽  
Vol 16 (6) ◽  
pp. 1158-1164 ◽  
Author(s):  
Jerome M. Seyer ◽  
Andrew H. Kang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Liver ◽  
Cyanogen Bromide ◽  
Terminal Segment ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Amino Terminal ◽  
Covalent Structure

Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB5 from type III collagen of human liver

Biochemistry ◽  
1980 ◽  
Vol 19 (8) ◽  
pp. 1583-1589 ◽  
Author(s):  
Jerome M. Seyer ◽  
Carlo Mainardi ◽  
Andrew H. Kang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Liver ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Covalent Structure

scholarly journals Haemoglobins of the Shark, Heterodontus Portusjacksoni II. Amino Acid Sequence of the a-Chain

1976 ◽  
Vol 29 (2) ◽  
pp. 73 ◽  
Author(s):  
AR Nash ◽  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Chromatography ◽  
Cyanogen Bromide ◽  
Gel Filtration ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Amino Terminal ◽  
Core Peptide ◽  
A Chain

The amino acid sequence of the a-chain of the principal haemoglobin from the shark, H. portusjacksoni has been determined. The chain has 148 residues and is acetylated at the amino terminal. The soluble peptides obtained by tryptic and chymotryptic digestion of the protein or its cyanogen bromide fragments were isolated by gel filtration, paper ionophoresis and paper chromatography. The amino acid sequences were determined by the dansyl-Edman procedure. The insoluble 'core' peptide from the tryptic digestion contained 34 residues and required cleavage by several proteases before the sequence was established. Compared with human a-chain there are 88 amino acid differences including the additional seven residues which appear on the amino terminal of the shark chain. There is also one deletion and one insertion. The chain contains no tryptophan but has four cysteinyl residues which is the highest number of such residues recorded for a vertebrate globin.

Repeated helical epitopes of defined amino acid sequence in human type III collagen identified by monoclonal antibodies

1992 ◽  
Vol 29 (6) ◽  
pp. 759-770 ◽  
Author(s):  
Hori Hisae ◽  
Douglas R. Keene ◽  
Lynn Y. Sakai ◽  
Mary K. Wirtz ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type
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