Partial purification and characterization of a trypsin-like proteinase from rabbit preimplantation uterine fluid.
Previous investigations have proved that proteinases are involved in implantation of the rabbit embryo into the uterine tissues. This study describes a trypsin-like enzyme found in the blastocyst fluid and uterine flushings at the time of implantation. The proteinase isolated from uterine flushings has a molecular mass of about 50 kDa and exists in two differently charged forms of pI 4.0 and 4.5. Tests with low molecular mass 4-nitroanilide substrates proved a marked cleavage selectivity of the enzyme for arginyl bonds. The catalytic activity is not affected by Ca2+ and EDTA but inhibited by aprotinin and a high concentration (10(-6)M) of lima bean trypsin inhibitor.
D000818:Animals; D001826:Body Fluids / Q000201:enzymology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D047108:Embryonic Development; D005260:Female; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007525:Isoelectric Focusing; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification*; D011247:Pregnancy; D011817:Rabbits; D014599:Uterus / Q000201:enzymology*
D010447:Peptide Hydrolases