Abstract:
:Two fractions of neutral alpha-glucosidase were partially purified from the insoluble fraction of bovine lens. This is the first report of such an event to the best of our knowledge. The apparent native molecular weights of these fractions were 121 kDa (fraction-I) and 254 kDa (fraction-II). Both fractions contained three polypeptides with molecular weights of 21, 25 and 30 kDa, although the proportion of these peptides was different in both fractions. The optimal pH of fraction-I and fraction-II was pH 6.0 and 6.5, and the optimal temperature for both fractions was approximately 50 degrees C. The Km values of fractions-I and -II for 4-methylumbelliferyl-alpha-glucopyranoside were 0.086, and 0.192 mM. The activities of these enzymes were inhibited strongly by HgCl2 and slightly by D-iodoacetic acid, but not by D-turanose. From this, we suggest that the enzyme in the insoluble fraction of bovine lens may be a cytoplasmic neutral alpha-glucosidase which binds to the cell membrane.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Kamei A,Fujiyama Odoi
10.1248/bpb.18.1133subject
Has Abstractpub_date
1995-08-01 00:00:00pages
1133-7issue
8eissn
0918-6158issn
1347-5215journal_volume
18pub_type
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