NDLI: Identification and primary structures of eel type I collagen proα1, proα2 and proα3

Content Provider	Springer Nature Link
Author	Saito, Masataka Higuchi, Tomoyuki Uchida, Naoyuki
Copyright Year	2014
Abstract	Many bony fish type I collagens have a characteristic third chain designated as α3(I). However, much less is known about the primary structure and distinction of the proα(I) chains. Their cDNAs were cloned by RT-PCR from the muscle tissue of Japanese eel, Anguilla japonica. Three cDNAs coding for the triple-helical domain of fibrillar collagen were identified as proα1(I), proα2(I) and proα3(I) chains by sequencing selected tryptic peptides isolated from eel type I collagen subunit chains, α1(I), α2(I) and α3(I). Eel proα3(I) had high amino acid sequence identity (81 %) to its proα1(I). The distribution of seven Cys residues in the C-propeptide of proα3(I) was identical to that of proα1(I). There was a third Cys residue at the 1,268th position from the N-terminus in proα1(I), though a supposed Cys residue at the 1,264th position in proα3(I) was replaced by a Ser residue. Similar replacement has been observed in the proα3(I) chains of trout and zebrafish. These combined results suggest that replacement of the Cys residue allows for the identification of fish collagen proα(I) previously not identified as proα3(I).
Starting Page	1323
Ending Page	1335
Page Count	13
File Format	PDF
ISSN	09199268
Journal	Fisheries Science
Volume Number	80
Issue Number	6
e-ISSN	14442906
Language	English
Publisher	Springer Japan
Publisher Date	2014-09-18
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	α3(I) Amino acid cDNA Collagen Fish Japanese eel structure Subunit Fish & Wildlife Biology & Management Freshwater & Marine Ecology Food Science
Content Type	Text
Resource Type	Article
Subject	Aquatic Science

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