Detail of "1136-89-6"

Reference

Isolation and characterization of electrophoretic variants of human prostatic acid phosphatase

Isolation and characterization of electrophoretic variants of human prostatic acid phosphatase. Hibbard, Michael D.; McCarthy, Robert C.; Markowitz, Harold (Dep. Lab. Med., Mayo Clin. and Mayo Found., Rochester, MN 55905, USA). Clin. Chem. (Winston-Salem, N. C.), 29(11), 1886-9 (English) 1983. CODEN: CLCHAU. ISSN: 0009-9147. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Prostatic acid phosphatase (EC 3.1.3.2) (I) purified from benign hypertrophic prostate tissue was fractionated by preparative slab isoelec. focusing over a pH gradient of 3.16-7.16. Of 29 fractions, 22 contained enzyme activity. Each active fraction was further examd. by detg. the Km and specific activity. 9001-77-8 and 1136-89-6 are also in the experiment. The protein concn. used in the latter detn. was estd. either spectrophotometrically or immunochem. by 3 different RIAs for I. The detn. of specific activities for each fraction directly correlated I activity with an immunochem. detn., which indicated the immunochem. relations among different mol. species of the enzyme. The Km values of the isolated fractions were similar to the Km values of purified unfractionated I. Most fractions analyzed by each immunoassay had similar specific activities; few fractions with discrepant specific activities were found at either end of the pH gradient. The similarity in specific activities among the fractions indicated that RIAs involving polyclonal antisera detected all of the electrophoretic variants of the enzyme. .

Inhibition of alkaline phosphatase activity by serum albumin

Inhibition of alkaline phosphatase activity by serum albumin. Foster, R. L.; Bannister, A. (Sch. Pharm., Liverpool Polytech., Liverpool, Engl.). Clin. Chem. (Winston-Salem, N. C.), 22(10), 1751-2 (English) 1976. CODEN: CLCHAU. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Increasing the serum albumin concn. in the assay medium for serum alk. phosphatase (I) caused a decrease in the hydrolysis rate of p-nitrophenyl phosphate and .alpha.-naphthyl phosphate, presumably due to binding of the substrates to albumin, as the protein concn. increased. For substrate concns. <1 mM, enzyme activity was inhibited, but this inhibition lessened as substrate concn.In this article, certain chemicals are used. Some of their cas registry numbers are 1136-89-6 and 330-13-2 increased, i.e., proportionately more substrate became available. At substrate concns. >1 mM, I was inhibited, but this inhibition was decreased by serum albumin. Kinetic anal. of the results showed .gtoreq.2 binding sites on albumin with assocn. consts. of .apprx.20 .times. 103/mole, compared to 5 .times. 103/mole for the enzyme active site. Although, at the concns. of serum protein normally introduced via the specimen into I assay medium contg. these substrates, this assocn. effect may not appreciably influence the rate, substrates and cofactors for clin. assays in general should have their assocn. consts. with other serum components checked, and standardization of serum diln. is a necessity for enzyme assays. .