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Characterization of type 1 collagen from the skin of blue grenadier (Marcruronus novaezelandiae)
Journal article   Peer reviewed

Characterization of type 1 collagen from the skin of blue grenadier (Marcruronus novaezelandiae)

J A M Ramshaw, J A Werkmeister and H A Bremner
Archives of Biochemistry and Biophysics, Vol.267(2), pp.497-502
1988
url
https://doi.org/10.1016/0003-9861(88)90056-2View
Published Version

Abstract

Biochemistry and Cell Biology
The skin collagen of a fish, blue grenadier (Macruronus novaezelandiae), has been purified and characterized. The fish skin was readily soluble in dilute acetic acid, with no pepsin treatment needed. The collagen was purified by salt precipitation. Skin samples from fish of various ages showed that even in the oldest sample, more than 8 years of age, the collagen was still readily acid soluble. The purified collagen had a melting temperature of 22 °C; the shrinkage temperature for the skin was 48 °C. Its tissue distribution, examined by immunohistology, and its chemical properties indicated a close homology to mammalian type I collagen. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that three distinct α-chains were present. These were purified by ion-exchange chromatography on CM-cellulose and by gel permeation chromatography on Superose 6. The three purified α-chain fractions were examined by amino acid analysis and by SDS-PAGE of their cyanogen bromide fragments. These data indicated that the additional chain was genetically distinct, and most closely related to the α1-chain, from which it was poorly resolved on SDS-PAGE.

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Biochemistry & Molecular Biology
Biophysics
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