Advances in Comparative Physiology and Biochemistry by O. Lowenstein

By O. Lowenstein

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Both general detection methods can lead to erroneous results. The en­ zyme elution method is subject to the pitfalls discussed in Section ΙΙ,Β. Similarly, zymograms produced by direct starch-iodine staining detect alb. o. a 1 2 3 4 5 T2 So TI h I Π III IV V FIG. 11. Diagrammatic representation of cattle serum protein patterns by one-dimen­ sional starch gel electrophresis. Only the anodic side of the gel is shown. Arrow indicates position of sample insertion. " Solid bands, intense staining; crosshatched, medium staining; dotted bands, faint or absent.

An analysis of the interaction of maltose and porcine pancreatic amylase by difference spectrophotometric and kinetic studies has im­ plicated a tryptophanyl side chain in the binding of substrate by the enzyme. , 1972). Using an alternative strategy, titration of the enzyme with residuespecific reagents has revealed t h a t sulfhydryl groups probably are not involved in enzyme catalysis (Greenwood and Milne, 1968), whereas histidyl residues probably are (Elödi, 1972). In the latter case, reaction of two histidyl residues with diethyl pyrocarbonate abolished catalytic activity but did not destroy the enzyme's ability to bind substrate ana­ logs.

Kikkawa (1953); Mukaiyama et al. S. S. I. I. I. I. I. S. S. I. I. S. I. I. Chesley (1934b); Kenyon (1925) Lehrner (1974); Lehrner and Malacinski (1975b); Malacinski and Rutter (1969) Griffiths (1965) Hope and Finnegan (1970) (Continued) 32 ROBERT C. KARN AND GEORGE M. I. I. I. I. S. I. I. Rajasingham et al. (1971); Neumann et al. I. Rajasingham et al. (1971) Rajasingham et al. I. I. I. Ettalibi et al. (1975) Hesselholt et al. 1966); Rajasingham et al. I. I. S. I. = Starch-iodine assay. Characteristics of α-glucosidase rather t h a n α-amylase (see text).

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