Studies on the proteinase of <i>Clostridium histolyticum</i>

Weil, L.; Kocholaty, Walter F.

doi:10.1042/bj0311255

Cited by 34 publications

(12 citation statements)

References 3 publications

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“…Van der Zant (1957) also observed a single peak of extracellular proteinase production for Pseudomonas putrefaciens. Weil and Kocholaty (1937) reported that secretion of an extracellular Figur-e 2. Elaboration of extracellular proteolytic enzymes by Pseudomnonas flutorescens when grown in tryptone-gluicosemeat extract broth at various temperatures.…”

Section: Resultsmentioning

confidence: 99%

Some Characteristics of Proteolytic Enzymes from Pseudomonas fluorescens1

Peterson¹,

Gunderson²

1960

Applied Microbiology

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Section: Resultsmentioning

confidence: 99%

Some Characteristics of Proteolytic Enzymes from Pseudomonas fluorescens1

Peterson¹,

Gunderson²

1960

Applied Microbiology

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“…This study supports the theory first advanced by Bersin and Longemann (14,15) which postulates that the activation of papain is due to the reduction of dithiol groups in the enzyme molecule) Other plant proteases which resemble papain in their activation and inhibition effects include those of the pineapple (3), fig (1), wheat (5), and Calotropis (16). On the other hand sulfhydryl apparently is not essential for the hydrolytic activity of the protease of pumpkin (3) and of several bacterial proteases (17,18).…”

Section: Activation and Inhibition Of Asdepainmentioning

confidence: 99%

Physicochemical Properties of the Proteolytic Enzyme From the Latex of the Milkweed, Asclepias Speciosa Torr. Some Comparisons With Other Proteases

Winnick

Davis

Greenberg

1940

Journal of General Physiology

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1. A study has been made of the properties of a hitherto unreported proteolytic enzyme from the latex of the milkweed, Asclepias speciosa. The new protease has been named asclepain by the authors. 2. The results of chemical, diffusion, and denaturation tests indicate that asclepain is a protein. 3. Like papain, asclepain dots milk and digests most proteins, particularly if they are dissolved in concentrated urea solution. Unlike papain, asclepain did not clot blood. 4. The activation and inhibition phenomena of asclepain resemble those of papain, and seem best explained on the assumption that free sulfhydryl in the enzyme is necessary for proteolytic activity. The sulfhydryl of asclepain appears more labile than that of papain. 5. The measurement of pH-activity curves of asclepain on casein, ovalbumin, hemoglobin, edestin, and ovovitellin showed no definite digestion maxima for most of the undenatured proteins, while in urea solution there were well defined maxima near pH 7.0. Native hemoglobin and ovovitellin were especially undigestible, while native casein was rapidly attacked. 6. Temperature-activity curves were determined for asclepain on hemoglobin, casein, and milk solutions. The optimum temperature was shown to increase with decreasing time of digestion.

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“…Manganese sulfate was added to the medium after it had been shown to give more rapid results, as suggested by the work of Levinson and Sevag (1954). The addition of cysteine or the substitution of cysteine and iron for the manganese, as suggested by the works of Weil and Kochalty (1937) and Kochalty et al (1938), did not result in a more rapid test. Likewise, the addition of 0.01 M calcium sulfate or its substitution for the manganese sulfate as suggested by the work of Lautrop (1956b), did not result in a more rapid test.…”

Section: Resultsmentioning

confidence: 99%