Purification, characterization, and expression of rat epididymal beta-D-galactosidase.
The purpose of the present study is to purify, kinetically characterize and measure the amount of soluble acid beta-D-galactosidase (EC 3.2.1.23) in different anatomical regions (caput, corpus, and cauda) of the adult rat epididymis. Based upon SDS-PAGE analysis, the subunit molecular mass of the caput and cauda enzyme is approximately 85,000 daltons while the corpus enzyme is approximately 50,000 daltons. The apparent Km and Vmax values are 67, 24, and 59 microM and 5.0, 1.88 and 6.3 microM/min./-mg protein for the enzyme purified from the caput, corpus, and cauda regions of the epididymis, respectively. However, no regional differences in the amount of soluble enzyme protein are observed. These data demonstrates regional differences in the activity of epididymal acid beta-D-galactosidase and suggest that the observed regional differences in enzyme activity may be due to posttranslational modifications.
Hall
J C
JC
Department of Biochemistry, North Carolina State University, Raleigh 27695-7622, USA.
Jacobetz
D R
DR
LaMarche
M D
MD
Kochins
J G
JG
Tubbs
C E
CE
D000818:Animals; D002850:Chromatography, Gel; D004790:Enzyme Induction; D004797:Enzyme-Linked Immunosorbent Assay; D004822:Epididymis / Q000201:enzymology* / Q000648:ultrastructure; D006031:Glycosylation; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D051381:Rats; D017207:Rats, Sprague-Dawley; D001616:beta-Galactosidase / Q000096:biosynthesis*
D001616:beta-Galactosidase