R Rytöluoto-Kärkkäinen

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Acid phosphatase activity of different parts (ventral, lateral and posterior lobes and coagulating gland) of the rat prostatic complex and seminal vesicles were analyzed in homogenate and after fractionation with gel filtration and chromatofocusing. Significant differences between the various tissue homogenates were recorded in the hydrolysis of(More)
The testicular homogenate of adult mice was eluted by DEAE-cellulose chromatography. Four peaks of acid phosphatase were identified. The pooled samples of each peak were used to determine substrate specificity, pH-optima, modifier characteristics, thermal stability, and Km-values. The results obtained suggest that each peak may represent a separate and(More)
Acid phosphatases of the rat ventral prostate were fractionated by gel filtration (GF) on Sepharose 6B, isoelectric focusing (IEF), and chromatofocusing (CF). In GF three activity peaks (GF-1, GF-2, GF-3) were disclosed. They showed some differences in substrate preference when six substrates (p-nitrophenyl phosphate; p-NPP; phenolphthalein phosphate,(More)
Four acid phosphatases were separated by gel filtration on Sepharose 6B and subsequent chromatography on DE-52 cellulose from human homogenate. The enzymes differed from each other in substrate preference, Km-values, modifier characteristics and molecular weights. The evidence obtained confirms that also in the human testis acid phosphatases of multiple(More)
Acid phosphatase activities were measured with five different substrates after fractionation with Sepharose 6B and DE-52 cellulose chromatography of homogenate from normal adult dog testis and a testicular tumor. The tumor showed a positive 3 beta-hydroxysteroid dehydrogenase reaction and was diagnosed as a Leydig cell adenoma. The fractionations gave three(More)
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