Chitin-bound protein of sarcophagid larvae: metabolism of covalently linked aromatic constituents

Sugumaran, M; Henzel, WJ; Mulligan, K; Lipke, H

HERO ID

5416604

Reference Type

Journal Article

Year

1982

Language

English

PMID

6295468

HERO ID 5416604
In Press No
Year 1982
Title Chitin-bound protein of sarcophagid larvae: metabolism of covalently linked aromatic constituents
Authors Sugumaran, M; Henzel, WJ; Mulligan, K; Lipke, H
Journal Biochemistry
Volume 21
Issue 25
Page Numbers 6509-6515
Abstract The borate-insoluble chitin-protein complex, CB-I, from prepupal sarcophagid larvae was cleaved with chymotrypsin and trifluoromethanesulfonic acid releasing a polypeptide fragment of Mr 68 000. The intact glycoprotein was blocked at the C terminus; the N-terminal sequence of Asp-Val-Ala-His-Tyr was not homologous with seven of the borate-soluble nonglycosylated structural proteins. Bityrosine was identified as a component of the primary chain, both half-residues occupied in peptide linkages. Sclerotization initiated a decline in bityrosine coincident with the addition of soluble proteins to the tanned matrix. The chitin-protein complex also included bound peroxidase, propolyphenol oxidase, and an o-diphenol subject to oxidation on activation of the zymogen. In the course of the oxidation N termini declined in accordance with the formation of 1,4 quinonoid cross-links.
Doi 10.1021/bi00268a029
Pmid 6295468
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English