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phosphomonoesterase/batata
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Purification of a ribonuclease from potato tubers and its use as an antigen in the immunochemical assay of this protein following tuber damage.
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A method for the purification of a ribonuclease from potato tubers is described. The preparation was free from deoxyribonuclease and phosphodiesterase activities and possessed only slight phosphomonoesterase activity. Specific antibodies against the ribonuclease preparation were raised in rabbits.
Increase in ribonuclease activity following mechanical damage to leaf and tuber tissues of Solanum tuberosum L.
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Major increases occurred in the capacity of damaged potato leaf and tuber tissues to hydrolyse ribonucleic acid whilst relatively minor increases were found in the activity of acid phosphomonoesterase and acid phosphodiesterase. Partial purification of homogenates by gel filtration on Sephadex G-100
Acid phosphatase of potato tubers (Solanum tuberosum L). Purification, properties, sugar and amino acid composition.
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1. Acid phosphatase (AcPase) from potato tubers was purified by tannic acid fractionation, DEAE-cellulose chromatography, filtration on Bio-Gel P-150 and affinity chromatography on Con A-Sepharose. The enzyme was purified 260-fold and was electrophoretically homogeneous; its mol. mass is about 69
Effect of pressure on plant endonuclease reactions.
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Effect of pressure on plant endonucleases, nuclease P1 from penicillium and an endonuclease from potato, was investigated especially on the influence on phosphomonoesterase and phosphodiesterase activities shown on substrates of XpYp type, as well as their intrinsic pressure-stability. The potato
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