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Yeasts asparaginase

Several factors are involved in the wide variation in tumor inhibitory activity of asparaginases from different sources (98). One obvious possibility is the rate of clearance of the enzyme from the circulation of the host animal, and Broome (26) was the first to obtain evidence implicating half-life as a factor in antitumor effectiveness. Guinea pig serum asparaginase, for example, has a half-life time of 11-19 hr, while a partially purified yeast asparaginase preparation without antilymphoma activity is almost completely cleared within 30 min. Differences in half-life alone cannot explain the differences in antitumor activity in all cases, however and the question still remains as to what structural features are responsible for rapid or slow clearance. Mashburn and Landin (85) have suggested that differences in half-life time may be related to the isoelectric point of the enzyme, and evidence also exists to support the idea that the tumor inhibitory activity of some asparaginases is related to their K, values (59, 67). [Pg.120]

Fig. 17.6. Experimental configuration for the integrated, primary purification of intracellular proteins from unclarified disruptates. Panel A configuration employed for the purification of G3PDH from baker s yeast. Elution was performed in packed bed mode under reversed flow. Panel B configuration for loading, wash and elution in fluidised bed mode (employed for the purification of L-asparaginase from Erwinia chrysanthemi). Fig. 17.6. Experimental configuration for the integrated, primary purification of intracellular proteins from unclarified disruptates. Panel A configuration employed for the purification of G3PDH from baker s yeast. Elution was performed in packed bed mode under reversed flow. Panel B configuration for loading, wash and elution in fluidised bed mode (employed for the purification of L-asparaginase from Erwinia chrysanthemi).
Several asparaginases from microorganisms were described prior to 1961. Asparaginase has been found in Aspergillus niger (22, 23), and is also present in yeasts (24 27). Extracts of Mycobacterium smegmatis,... [Pg.103]

Enzymes. The clinical utility of L-asparaginase has acted as a stimulus for the evaluation of other enzymes for possible antitumor activity. A phenylalanine ammonia-lyase from yeast rapidly decreased the plasma phenylalanine and tyrosine... [Pg.143]


See other pages where Yeasts asparaginase is mentioned: [Pg.117]    [Pg.28]    [Pg.41]    [Pg.117]    [Pg.28]    [Pg.41]    [Pg.409]    [Pg.410]    [Pg.391]    [Pg.105]    [Pg.272]    [Pg.131]    [Pg.132]    [Pg.211]    [Pg.108]    [Pg.636]    [Pg.193]    [Pg.342]    [Pg.26]    [Pg.651]   
See also in sourсe #XX -- [ Pg.103 , Pg.117 ]




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