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A comparison of some properties of human red cell acid phosphatase in different phenotypes
Author(s) -
Luffman JILL E.,
HARRIS HARRY
Publication year - 1967
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1967.tb00040.x
Subject(s) - thermostability , chemistry , hydrolysis , acid phosphatase , biochemistry , glycerol , urea , ethanol , substrate (aquarium) , guanidine , enzyme , methanol , chromatography , biology , organic chemistry , ecology
Summary 1. The red cell acid phosphatase types A, BA, B, CA and CB have been compared with respect to a number of different properties. 2. Types CA and CB have been found to be relatively much more thermostable than types B, BA and A. In the latter group, type B appears to show slightly greater thermostability than type A and type BA appears to be intermediate in this respect. 3. No significant differences between the types were found in denaturation by guanidine or urea. 4. Phosphotransferase activity determined with PNPP as substrate and methanol as acceptor, and expressed as percentage of hydrolytic activity in the absence of the alcohol, appeared to be much the same in the different types. A similar result was obtained when glycerol, propanol and ethanol were used as acceptors. The greatest phosphotransferase activities (more than three times the hydrolytic activities) were observed with glycerol and methanol in concentrations of 20–26%. 5. No marked differences between the types in the pattern of substrate specificity were detected. 6. Considerable retardation of red cell acid phosphatase in gel atration using Biogel P‐60 was observed. The elution peak emerged from the column subsequent to myoglobin and cyto‐chrome c markers. This suggests that the enzyme may have a relatively low molecular weight. Similar results were obtained with each type.