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Pancreatic chain-length specificity

Human milk lipase and human gastric lipase have specificities similar to pancreatic lipase and hydrolyze tributyrin more rapidly than other triglycerides (240, 243). Triglycerides with a chain length of four to eight carbon atoms are hydrolyzed most rapidly by Ricinus lipase (146). Specificity similar to pancreatic lipase is shown by the lipase of Penicil-litim roqueforti (244), but the lipase of Aspergillus hydrolyzes tricaprylin and triolein more rapidly than tributyrin (244). [Pg.210]

The specificity of pancreatic RNAse is such that any change of purine for pyrimidine (or the converse) in an rRNA molecule will give an alteration in the chain length of the digestion product. Within the limits of sensitivity of such a double-label experiment (about 5%), no detectable transitions occurred between bound and free 26 S rRNA. [Pg.179]


See other pages where Pancreatic chain-length specificity is mentioned: [Pg.136]    [Pg.235]    [Pg.1896]    [Pg.199]    [Pg.69]    [Pg.473]    [Pg.647]    [Pg.256]    [Pg.647]    [Pg.1855]    [Pg.36]    [Pg.37]   
See also in sourсe #XX -- [ Pg.136 ]




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Chain length specificity

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