Ribonuclease-RNAase inhibitor complex from rat testis. Purification of the RNAase inhibitor.
The RNAase inhibitor from rat testis has been purified to homogeneity. The purified protein appeared as a single spot after two-dimensional electrophoresis. The calculated Mr value is 48,000 which coincides with that obtained for the native protein on gel filtration chromatography, thus indicating a single polypeptide chain. The amino acid composition and the characteristics of the inhibitor activity are reported and compared to those of other RNAase inhibitors from mammalian tissues. The naturally occurring ribonuclease-RNAase inhibitor complex from rat testis has also been studied and compared with the rat testis inhibitor-RNAase A as model complex. The ribonuclease released from the natural rat testis complex showed heterogeneity of size. The significance of the rat testis ribonuclease/RNAase inhibitor system is discussed in terms of the important functionality of this organ.
Fominaya
J M
JM
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain.
García-Segura
J M
JM
Gavilanes
J G
JG
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D006801:Humans; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009928:Organ Specificity; D011485:Protein Binding; D011506:Proteins / Q000302:isolation & purification* / Q000502:physiology; D051381:Rats; D011919:Rats, Inbred Strains; D012260:Ribonucleases / Q000037:antagonists & inhibitors*; D013045:Species Specificity; D013737:Testis / Q000201:enzymology*
D000596:Amino Acids; D004791:Enzyme Inhibitors; D011506:Proteins; D012260:Ribonucleases