Pintip RuenwongsaMontri ChulavatnatolMahidol University2018-04-192018-04-191974-07-10Biochemical and Biophysical Research Communications. Vol.59, No.1 (1974), 44-50109021040006291X2-s2.0-0016231341https://repository.li.mahidol.ac.th/handle/20.500.14594/10603A new acidic protease with pH optimum of 3.0 was partially purified from human seminal plasma. It can hydrolyze hemoglobin and N, N-dimethyl casein. It was stable in acidic but labile in neutral and alkaline solutions. Its molecular weight was determined by gel filtration to be 40,000. Its chromatographic behavior on carboxy methyl Sephadex column was quite different from the pH-8.0 protease of human seminal plasma. It was present in seminal plasma of normal and vasectomized individuals. Its activity was not affected by cysteine, metal cations or ethylene diamine tetraacetic acid. © 1974 Academic Press, Inc.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/S0006-291X(74)80171-3