The Covalent Structure of Calf Skin Type III Collagen. I. The Amino Acid Sequence of the Amino Terminal Region of the αl(III) Chain (Position 1-222)

1979 ◽  
Vol 360 (2) ◽  
pp. 809-868 ◽  
Author(s):  
Peter P. FIETZEK ◽  
Hartmut ALLMANN ◽  
Jürgen RAUTERBERG ◽  
Werner HENKEL ◽  
Elmar WACHTER ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Region ◽  
Skin Type ◽  
Collagen I ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Amino Terminal ◽  
Covalent Structure ◽  
Calf Skin

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 Complete amino acid sequence of the N-terminal extension of calf skin type III procollagen

1984 ◽  
Vol 219 (2) ◽  
pp. 625-634 ◽  
Author(s):  
A Brandt ◽  
R W Glanville ◽  
D Hörlein ◽  
P Bruckner ◽  
R Timpl ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type Iii Collagen ◽  
Type I ◽  
Globular Domain ◽  
Type Iii ◽  
Type I Procollagen ◽  
Type Iii Procollagen ◽  
Calf Skin

The N-terminal extension peptide of type III procollagen, isolated from foetal-calf skin, contains 130 amino acid residues. To determine its amino acid sequence, the peptide was reduced and carboxymethylated or aminoethylated and fragmented with trypsin, Staphylococcus aureus V8 proteinase and bacterial collagenase. Pyroglutamate aminopeptidase was used to deblock the N-terminal collagenase fragment to enable amino acid sequencing. The type III collagen extension peptide is homologous to that of the alpha 1 chain of type I procollagen with respect to a three-domain structure. The N-terminal 79 amino acids, which contain ten of the 12 cysteine residues, form a compact globular domain. The next 39 amino acids are in a collagenase triplet sequence (Gly- Xaa - Yaa)n with a high hydroxyproline content. Finally, another short non-collagenous domain of 12 amino acids ends at the cleavage site for procollagen aminopeptidase, which cleaves a proline-glutamine bond. In contrast with type I procollagen, the type III procollagen extension peptides contain interchain disulphide bridges located at the C-terminus of the triple-helical domain.

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