1970
DOI: 10.1021/bi00813a016
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Water-insoluble enzymes. Synthesis of a new carrier and its utilization for preparation of insoluble derivatives of papain, trypsin, and subtilopeptidase A

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Cited by 91 publications
(20 citation statements)
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“…This effect can be due to the positively charged unsubstituted amidino groups on the polymer [12,13]. It should be noted that the pH-activity profile for bound urease is broader than that for the corresponding free enzyme [14], as shown in Fig.2.…”
Section: Resultsmentioning
confidence: 99%
“…This effect can be due to the positively charged unsubstituted amidino groups on the polymer [12,13]. It should be noted that the pH-activity profile for bound urease is broader than that for the corresponding free enzyme [14], as shown in Fig.2.…”
Section: Resultsmentioning
confidence: 99%
“…It was shown that the pH-activity prof'des of polyanionic derivatives of several proteolytic enzymes, such as the ethylene maleic acid copolymer derivative of trypsin, are displaced by 1 to 2.5 pH units towards the alkaline side as compared to the native enzyme [42]. Polycationic derivatives of the same enzyme exhibited the reverse behavior displacing the pH optimum to more acidic pH values [43].…”
Section: Microenvironmental Matrix-effectsmentioning
confidence: 99%
“…However, the adsorption is quite low and most of the ALP in the other experiments will be present in an immobilized form onto the support by a covalent linkage through the carbonate groups. 5.0 mL in 0.05M glycine buffer at pH 9; enzyme concentration 2.0 mg/mL; temperature 4OC.…”
Section: Immobilization Of Alkaline Phosphatase (Alp) Onto Pvca-jeff mentioning
confidence: 99%