type	Journal Article
authors	Kraus, J. P.; Rosenberg, L. E.
title	Cystathionine beta-synthase from human liver: improved purification scheme and additional characterization of the enzyme in crude and pure form
journal	Arch Biochem Biophys
Activity	4.2.1.22
ui	83177108
year	(1983)
volume	222
number	1
pages	44-52.
keywords	Amino Acids/isolation & purification
abstract	The previously published procedure (Kraus et al. (1978) J. Biol. Chem. 253, 6523-6528) for the purification of cystathionine beta-synthase [L- serine hydro-lyase (adding homocysteine) EC 4.2.1.22], a pyridoxal 5'- phosphate-dependent enzyme from human liver has been modified. The new procedure, starting with a liver homogenate "aged" for 7 days at 4 degrees C, yielded homogeneous enzyme purified over 3000-fold with a much improved yield. "Aging" of the enzyme in crude homogenates yields a form apparently smaller by gel electrophoresis and with significantly increased activity and antigenicity. This species of cystathionine beta- synthase does not form stable complexes with other proteins during purification as does the previously employed, freshly used species. An absorption spectrum and an amino acid composition of the pure enzyme were determined; the amino-terminal residue was shown to be methionine. The isoelectric points of holosynthase and aposynthase were estimated to be 5.2 and 5.6, respectively. Rabbit antiserum raised against the pure cystathionine beta-synthase was characterized using as antigen crude synthase from five different mammalian species as well as the pure human enzyme.
last changed	2002/11/12 16:17