![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Abstract
Acid phosphatase activities were measured with five different stubstrates in the total homogenates as well as after gel filtration on Sepharose 6B and cellulose chromatography of bull, guinea pig, rabbit, and ram testes. The response of the hydrolysis rate to NaF (5 mmol/1), Co2+ (5 mmol/1) and Zn2+ (5 mmol/1) was also tested. In the total homogenate the hydrolysis of p-nitrophenyl phosphate was markedly activated by Co2+, while in the presence of Zn2+ an activation was recorded in guinea pig and some inhibition in the bull, rabbit, and ram testes. NaF caused a decline in the total acid phosphatase activity, particularly in guinea pig and ram. The gel filtration resulted in three separate activity peaks with p-NPP and β-NP as substrates. N-ASBI-P, α-NP, and Tym-P gave only two peaks. After subsequent cellulose chromatography of the activities only peak II gave rise to two further activities. Peak I of gel filtration (enzyme I) was able to hydrolyze all substrates tested and was highly sensitive to NaF. Peak I of cellulose chromatography (enzyme II) also hydrolyzed all substrates and was sensitive to NaF. Peak III of gel filtration (enzyme III) hydrolyzed p-NPP and β-NP. It was rather resistant to NaF but sensitive to Zn2+. It was slightly activated by Co2+. Peak II of cellulose chromatography (enzyme IV) hydrolyzed only p-NPP and was markedly activated by Co2+ and Zn2+. The adult testes of bull, guinea pig, rabbit, and ram have a closely similar testicular acid phosphatase pattern. Due to relative differences in the concentrations of the four enzymes in the tissue, varying activity levels are recorded in the presence of different substrate and modifier combinations.