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Study on Basic Arginine Amidase in Human Seminal Plasma

대한산부인과학회지 1993년 36권 4호 p.473 ~ 482
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Abstract


Three arginine amidase activities having different molecular weights were detected and separated from human seminal plasma by gel filtration on a Cellulofine GCL-2000 gel column and a Lima Bean Trypsin Inhibitor (LBTI) affinity column. They were
tentatively called high, middle and low molecular weight (HMW-, MMW- and LMW-) arginine amidases. The substrate specificity of MMW- and LMW- arginine amidases showed in good agreement with basic arginine amidases from human male urine -1 and
-2(BHUAE-1
and-2), respectively.
Basic arginine amidase in MMW-arginine amidase preparation of human seminal plasma was purified about 232-from initial purified human seminal plasma by CM-cellulose adsorption and chromatography, and LBTI-affinity adsorption and elution and this
enzyme
was homogeneous on SDS polyacrylamide gel electrophoresis. The specific activity of Tos-Arg-Me esterolysis was 3.2 μmol/minA280 and properties of this enzyme were different from some proteinases in semen such as acrosin, tissue kallikrein and
seminine.
.

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