Download e-book for iPad: Advances in Comparative Physiology and Biochemistry by O. Lowenstein

By O. Lowenstein

ISBN-10: 0120115077

ISBN-13: 9780120115075

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1 9 6 9 ) . Biochemistry 8, 4 3 8 2 - 4 3 9 0 . ] may occur is available. In purifying D. hydei amylase-7 and -8, how­ ever, Doane et al. (1975) have observed the appearance of more anodal isozymes and a single more cathodal isozyme (Fig. 15). They specu­ lated that the more anodal isozymes might arise by deamidation as has been noted for human (Keller et al, 1971; Kam et al, 1975) and chicken (Lehrner, 1974; Lehrner and Malacinski, 1975a,b) amylases. Work with vertebrates has revealed complex relationships among the amylase isozymes of the various tissues and fluids examined.

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). 20), a common lysosomal acid hydrolase which is an exoamylase.

13). They noted multi­ ple forms in all but the pancreas of the guinea pig and the salivary glands of chicken, beef, and rabbit. Rajasingham et al. (1971) compared mammalian amylases by disc electrophoresis followed by indirect staining on starch plates (Fig. 14). In comparing saliva, serum, urine, pancreatic extracts, and extracts of the small intestine, they found multiple electrophoretic forms in nearly all sources. Specific studies employing a variety of electrophoretic techniques have revealed fur­ ther heterogeneity in many of these organisms.

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Advances in Comparative Physiology and Biochemistry by O. Lowenstein


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