| Literature DB >> 667115 |
K M Fukasawa, K Fukasawa, M Harada.
Abstract
Dipeptidyl aminopeptidase IV was purified 350 fold from pig kidney by chromatographic procedures including affinity chromatography with conjugates of Gly-Pro linked to Sepharose 4.B. Purified enzyme existed in a dimeric form as determined by sodium dodecyl sulfate polyacrylamide-gel electrophoresis using dimethyl suberimidate (a cross-linking reagent). The molecular weight of the subunit was estimated to be 100 000 by gel filtration with 6 M guanidine hydrochloride and to be 94 000 based on analysis of N-terminal residue (dinitrophenyl-serine). The amino acid composition of the purified enzyme was also determined. The enzyme contained 18.3% of carbohydrate consisting of mannose, galactose, fucose, glucosamine and sialic acid. The enzyme desialized with sialidase was found to still possess full enzyme activity.Entities:
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Year: 1978 PMID: 667115 DOI: 10.1016/0005-2795(78)90042-9
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002