Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB9 from type III collagen of human liver

Biochemistry ◽  
1981 ◽  
Vol 20 (9) ◽  
pp. 2621-2627 ◽  
Author(s):  
Jerome M. Seyer ◽  
Andrew H. Kang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Liver ◽  
Type Iii Collagen ◽  
Type Iii ◽  
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

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

Inhibition by Peptidic Fragments of Clq of Platelet - Collagen Interactions

1979 ◽  
Author(s):  
J.L. wautier ◽  
K.B.M. Reid ◽  
Y. Legrand ◽  
J.P. Caen
Keyword(s):  
Amino Acid ◽  
Platelet Aggregation ◽  
Amino Acid Sequence ◽  
Platelet Adhesion ◽  
Type Iii Collagen ◽  
Type I ◽  
Inhibit Platelet Aggregation ◽  
Pepsin Digestion ◽  
Type Iii ◽  
Collagen Peptides

Clq (first component of complement) has been shown to inhibit platelet aggregation induced by collagen. Platelet aggregation and adhesion to purified type I or type III collagen have been studied in the presence of various fragment of Clq.The collagen like region was obtained by digestion of Clq by pepsin and by isolation of the fragments by chromatography on sephadex G 200. The globular region was prepared by digestion of Clq by collagenase, and filtration. The collagen like region is as effective as native Clq in inhibiting platelet aggregation or adhesion in the presence of type I or type III collagen, while the globular region was without effect.Using peptides obtained from the collagen like region of Clq (reduction and alkylation, performic oxidation, CNBr treatment, extensive pepsin digestion) it could be shown that the fragment (FR II = 70 Amino Acid) was responsible for the inhibition of the platelet adhesion and aggregation induced by type I or type III collagen.The Amino Acid sequence of this fragment was compared to the known sequence of the collagen peptides involved in platelet adhesion (see Fauvel et al).

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.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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