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  • Author or Editor: Ronald R. Minor x
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Summary

Collagen type I was purified from equine skin and flexor tendon, and type II collagen was purified from equine articular cartilage. The proteoglycans in these tissues were extracted, using guanidine hcl; the collagens were solubilized, using pepsin digestion, then were selectively precipitated with NaCl. Gel electrophoresis indicated that the precipitates contained only type I or type II collagen. Amino acid analysis indicated that collagen constituted > 97% of the total protein in the precipitates. Hydroxylation of proline was 42.0 ± 0.6% (mean ± sem) in α1(I) and α2(I), and was 48.1 ± 1.3% in α1(ID chains. The hydroxylation of lysine was 23.2 ± 0.7% in α1(I) and 34.1 ± 0.9% in α2(D) chains from tendon, and 49.6 ± 4.3% in a1( chains from cartilage. The cyanogen bromide (CB)-peptide patterns of chromatographically purified equine α2(I) and α1(II) chains were similar to those published previously for rat, bovine, and human α2 and α1 chains. However, the CB-peptide pattern of the equine α1(I) chain resembled the guinea pig α1(I) chain, which has no methionine between CB7 and CB6. Purified equine α1(I)CB7,6 contained no methionine, methionine sulfoxide, or homoserine lactone. Mass of 42.26 kd was determined by use of mass spectrometry, and N-terminal sequence analysis established that the first 12 amino acids of this CB7,6 were identical to the sequence of human α1(I)CB7. Because of this species specific difference in structure of the α1(I) chain, equine CB-peptides should be used as standards in studies of variations in the proportions of type I and type II collagens in equine tissues expressing the phenotype of fibrous tissue and cartilage.

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in American Journal of Veterinary Research