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- W1980745002 abstract "Abstract Glycopeptides from larval, white puparial and fully sclerotized cuticle were prepared by four different routes and amino acid composition compared. Uniformly high levels of glycine characterized larval material whereas glutamic acid predominated following sclerotization. Increased titres of lysine also distinguished the puparial case. This relationship obtained for samples prepared by cleavage with (a) N-bromosuccinimide, (b) hydrochloric-formic acids, (c) alkali-borohydridenitrous acid and (d) sodium in liquid ammonia. The formation of puparial-type peptidochitodextrins occurred early in the puparial transformation based on the presence of both glutamic acid-rich and glycine-rich glycopeptides in the intermediate white puparial stage. Sclerotized cuticle retained some glycine-rich material although peptides enhanced with respect to glutamic acid and lysine clearly predominated. Exhaustive digestion with proteolytic enzymes did not alter amino acid mole ratios. Attempts to cleave glycopeptides chemically or with chitinase were also unsuccessful as a means of identifying the amino acid linked to chitin. Since the two components deposited during pupariation, namely β-alanine and polyphenol, were not detected in the limit glycopeptides from sclerotized cuticle, failure to effect complete proteolysis is ascribed to the shielding action of chitinase-resistant poly-N-acetylglucosamine chains, rather than the presence of these protease-insensitive substituents in the peptide moiety. Assuming peptides of similar length obtain following identical degradative procedures, a greater number of links between polysaccharide and protein characterize puparial integument, since amino acid/amino sugar ratios are higher following sclerotization by a factor of 2 or more." @default.
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- W1980745002 date "1976-01-01" @default.
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- W1980745002 title "Peptodochitodextrins of Sarcophaga bullata: Non-identity of limit glycopeptides from larval and puparial cuticle" @default.
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