Biomaterial Database

Some characteristics and cellular distribution of phospholipases A1 and A2 of rat testis. 1982

L R Chaudhary

The subcellular distribution and some properties of different phospholipases A of rat testis were studied using exogenous 1-acyl-2-[1-14C] oleoyl-sn-glycerol-3-phosphocholine as substrate. The presence of distinct phospholipases A: two phospholipases A1 with pH optimum at 3.0 and 7.4 respectively and a phospholipase A2 with pH optimum at 7.4 has been shown. The neutral phospholipases A1 and A2 have been further studied. The activities of phospholipases A1 and A2 with a pH optimum of 7.4 were greatly stimulated by sodium deoxycholate but were not affected by Triton X-100. The enzyme activities were slightly stimulated by Ca2+ but inhibited by EDTA at higher concentration. Studies using various effecters showed that the phospholipase A1 and A2 were, sensitive to sulfhydryl reagents and heat, insensitive to DIFP and cyclic nucleotides and completely inhibited by sodium dodecyl sulfate. Subcellular fractionation of testis homogenates and the subcellular distribution patterns of markers, marker enzymes and phospholipases A indicated that the phospholipases A1 and A2 with highest specific and relative specific activities were mainly localized in microsomal fractions.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008297	Male		Males
D008861	Microsomes	Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)	Microsome
D010740	Phospholipases	A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-.	Lecithinases,Lecithinase,Phospholipase
D010741	Phospholipases A	Phospholipases that hydrolyze one of the acyl groups of phosphoglycerides or glycerophosphatidates.
D006358	Hot Temperature	Presence of warmth or heat or a temperature notably higher than an accustomed norm.	Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot
D006863	Hydrogen-Ion Concentration	The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH	pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013347	Subcellular Fractions	Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)	Fraction, Subcellular,Fractions, Subcellular,Subcellular Fraction
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities