Different forms of renin in the kidney and their relations were investigated by gel-filtration with sephadex G-75. Low molecular weight renin (M.W. 45, 000) was found in both of intact Wistar-Kyoto rat (WKY) and WKY whose renin-angiotensin system was stimulated by adre-nalectomy and feeding no salt diet, by extracting with 0.05M pyrophosphate buffer, at pH 6.5. An addition of 10mM N-ethylmaleimide (NEM) to the buffer did not change the molecular weight of renin extracted.
From human cadaver kidney, low molecular weight renin (M.W. 45, 000) was extracted by the same procedure.
In hog kidney, on the other hand, high molecular weight renin (M.W. 67, 000) was extracted with 0.05M pyrophosphate buffer, at pH 6.5. High molecular weight renin (M.W. 67, 000) was extracted also with the buffer containing 10mM tetrathionate (TT), a sulfhydryl blocker. However, with the same buffer containing another sulfhydryl blocker, NEM, low molecular weight renin (M.W. 45, 000) was extracted. With the buffer containing a sulfhydryl compound, 100mM dithiothreitol (DTT), low molecular weight renin (M.W. 45, 000) was extracted. When NEM was added to the high molecular renin extracted with 0.05M pyrophosphate buffer, approximately a half of the renin was converted to low molecular weight renin. After acidification to pH 3.3 for 10min, the high molecular weight renin was converted to low molecular weight renin.
The results were against the assumption that a sulfhydryl requiring enzyme (SH-enzyme) participated in the interconversion between high molecular weight renin and low molecular weight renin.
It is reasonable to assume that the actions of NEM, TT, and DTT are not through a SH-enzyme, but affect directly the interconversion of sulfhydryl group and disulfide (S-S) bond which exists in the renin molecule, and high molecular weight renin may be formed by a combination of low molecular weight renin and another protein with a S-S bond(s).
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