Role of carbohydrate in rat plasma thiostatin: deglycosylation destroys cysteine proteinase inhibition activity.
Rat plasma thiostatin, a 68kDa glycoprotein cysteine proteinase inhibitor, was chemically deglycosylated with trifluoromethanesulfonic acid. Both native and deglycosylated species were characterized with regard to amino acid and carbohydrate composition, homogeneity by SDS-PAGE, immunoreactivity by Western blot, and cysteine proteinase inhibitor activity. Deglycosylation of thiostatin did not alter the integrity of the protein backbone nor change the immunologic recognition of the molecule by polyclonal rabbit anti-rat thiostatin. However, deglycosylation did destroy cysteine proteinase inhibitor activity activity as measured against papain.
Rusiniak
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ME
Department of Biochemical Pharmacology, School of Pharmacy, State University of New York, Buffalo 14260.
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D000818:Animals; D015153:Blotting, Western; D002241:Carbohydrates / Q000737:chemistry*; D015853:Cysteine Proteinase Inhibitors; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006031:Glycosylation; D007704:Kininogens / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification; D008297:Male; D008698:Mesylates / Q000737:chemistry; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D013329:Structure-Activity Relationship
D002241:Carbohydrates; D015853:Cysteine Proteinase Inhibitors; D007704:Kininogens; D008698:Mesylates; C012077:trifluoromethanesulfonic acid