Placenta-like alkaline phosphatases from human osteosarcoma cells

Hormone-induced alkaline phosphatases in human osteosarcoma cells (LM) were extracted and purified. Characterization of the purified enzyme showed two distinct isoenzymes. One isoenzyme was heat labile, was homoarginine inhibited, and had the electrophoretic migration of alkaline phosphatase of huma...

Full description

Saved in:
Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 1978-01, Vol.38 (1), p.193-198
Main Authors: Singh, I, Tsang, K Y, Blakemore, W S
Format: Article
Language:English
Subjects:
Alkaline Phosphatase - antagonists & inhibitors
Alkaline Phosphatase - biosynthesis
Alkaline Phosphatase - metabolism
Bone and Bones - enzymology
Cells, Cultured
Enzyme Induction - drug effects
Female
Hot Temperature
Humans
Hydrocortisone - pharmacology
Hydrogen-Ion Concentration
Isoenzymes - metabolism
Neoplasms, Experimental - enzymology
Osteosarcoma - enzymology
Phenylalanine - pharmacology
Placenta - enzymology
Pregnancy
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Hormone-induced alkaline phosphatases in human osteosarcoma cells (LM) were extracted and purified. Characterization of the purified enzyme showed two distinct isoenzymes. One isoenzyme was heat labile, was homoarginine inhibited, and had the electrophoretic migration of alkaline phosphatase of human osseous origin. Immunodiffusion showed that this isoenzyme reacted positively only against anti-bone alkaline phosphatase antibodies. The second isoenzyme was heat stable, was inhibited by phenylalanie, and had the same electrophoretic migration as did alkaline phosphatase extracted from mature normal human placenta. This second isoenzyme had the same antigenicity as did the normal placental enzyme. Like the D-variant placental phenotype, this second isoenzyme was inhibited by L-leucine and ethylenediaminetetraacetic acid.
ISSN:0008-5472