Detail of "3150-24-1"

Reference

Glucosylation of p-nitrophenol by hepatopancreas of Homarus americanus

Glucosylation of p-nitrophenol by hepatopancreas of Homarus americanus. Elmamlouk, T. H.; Gessner, T. (Biochem. Pharmacol. Dep., State Univ. New York, Buffalo, N. Y., USA). Xenobiotica, 7(1-2), 111-2 (English) 1977. CODEN: XENOBH. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) Hepatopancreas homogenates of H. americanus converted p-nitrophenol [100-02-7] to its glucoside conjugate in the presence of UDP-glucose, the activity being largely in the microsomes. P-nitrophenol galactoside [3150-24-1] was probably formed in the presence of UDP-galactose but the glucuronide conjugate was not formed in the presence of UDP-glucuronic acid. The microsomal glucosyltransferase had a pH optimum of 7.9-8.1 showed increased activity as the temp. was raised from 5 to 45.degree.. P-nitrophenol concns. >3mM caused substrate inhibition.

Purification and properties of two

Purification and properties of two .beta.-glycosidases from Cicer arietinum L. with preferential specificity for biochanin A 7-.beta.-apiosylglucoside. Hoesel, Wolfgang (Univ. Muenster, Muenster, Ger.). Hoppe-Seyler's Z. Physiol. Chem., 357(12), 1673-81 (German) 1976. CODEN: HSZPAZ. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Four different .beta.-glycosidases were sepd. from leaves of chick pea plants, C. arietinum, by DEAE-cellulose chromatog. One was specific for isoflavone 7.beta.-glucosides. Two others showed very similar protein properties and identical catalytic activities. They were further purified and both appeared as single, homogeneous protein bands after alk. disc electrophoresis and isoelec. focusing. Isoelec. points were at pH 4.35 and 4.45, resp. Both .beta.-glycosidases had mol. wts. of 120,000-140,000 and had 2 subunits with indentical mol. wts. of 65,000. Both .beta.-glycosidases preferentially catalyzed hydrolysis of diglycosides like biochanin A 7.beta.-apiosyl(1.fwdarw.2)glucoside (Km = 1.5 .times. 10-4M; V = 10 .mu.mol min-1 mg-1). The apiosylglucoside unit was liberated as an intact disaccharide. . 3150-24-1 and 15914-68-8 which are cas registry numbers of chemicals are mentioned.beta.-Glucosides, such as biochanin A 7.beta.-glucoside or 2-nitrophenyl glucoside, were also efficiently hydrolyzed. The .beta.-glycosidases also possessed transferase activity, but only when measured with isoflavone aglycones as acceptors. Transfer of the intact apiosylglucoside unit of biochanin A 7.beta.-apiosylglucoside was demonstrated. The enzymes had a pH optimum of 5.5. The .beta.-glycosidases were strongly inhibited by p-hydroxymercuribenzoate and Bromocondurite. Glucono-1,5-lactone, Ag+, and Hg2+ showed only weak inhibition and Condurit B epoxide had no effect. At 4th .beta.-glycosidase activity from chick pea leaves showed no preferential activity for isoflavone 7-glycosides. .