TY - JOUR
T1 - Alkaline phosphatase. I. Comparison of the physical and chemical properties of enzyme preparations from mammalian cell cultures, various animal tissues, and Escherichia coli
AU - Cox, Rody P.
AU - Griffin, Martin J.
N1 - Funding Information:
1 This investigation was supported by contract U-1296 of the Health Research of the City of New York, and genetics grant No. 5Tl HE 5307 of the United States Health Service. 2 Career Scientist of the Health Council of the City of New York. 3 Postdoctoral Genetics Trainee; dress: Oklahoma Medical Research Oklahoma City.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1967/12
Y1 - 1967/12
N2 - Some of the chemical and physical properties of alkaline phosphatase preparations derived from mammalian tissues, cell cultures, and E. coli have been compared. A number of chemical and physical properties of the various enzyme preparations are similar, such as the concentration of cysteine and histidine that inhibits alkaline phosphatase activity, and the phosphotransferase activity of different enzyme preparations. Other properties of the various alkaline phosphatases are markedly different, such as heat stability at 56 °, electrophoretic mobility, and the concentrations of Zn ions, L-phenylalanine, and L-tryptophan required to inhibit enzyme activity by 50%. These differences provide a means of distinguishing between alkaline phosphatases from different tissues and different species. Some of the physical and chemical characteristics of these enzymes appear to be related to, or coincidently associated with the mechanisms of enzyme regulation observed in cell cultures and in vivo.
AB - Some of the chemical and physical properties of alkaline phosphatase preparations derived from mammalian tissues, cell cultures, and E. coli have been compared. A number of chemical and physical properties of the various enzyme preparations are similar, such as the concentration of cysteine and histidine that inhibits alkaline phosphatase activity, and the phosphotransferase activity of different enzyme preparations. Other properties of the various alkaline phosphatases are markedly different, such as heat stability at 56 °, electrophoretic mobility, and the concentrations of Zn ions, L-phenylalanine, and L-tryptophan required to inhibit enzyme activity by 50%. These differences provide a means of distinguishing between alkaline phosphatases from different tissues and different species. Some of the physical and chemical characteristics of these enzymes appear to be related to, or coincidently associated with the mechanisms of enzyme regulation observed in cell cultures and in vivo.
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U2 - 10.1016/0003-9861(67)90158-0
DO - 10.1016/0003-9861(67)90158-0
M3 - Article
AN - SCOPUS:0004338630
SN - 0003-9861
VL - 122
SP - 552
EP - 562
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 3
ER -