Download Advances in Comparative Physiology and Biochemistry by O. Lowenstein PDF

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By O. Lowenstein

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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.

1964). It is generally believed t h a t calcium does not directly participate in the catalytic process but r a t h e r t h a t it is in­ volved in stabilizing the tertiary structure of the active enzyme. Other ions, such as chloride, are also required for maximal enzyme activity. Optimal concentrations of chloride ions (approx. , 1947). IV. TISSUE AND ORGAN DISTRIBUTIONS A. Secretory Organs Many species representing nearly all the phyla in the animal king­ dom have been studied for amylase content and its tissue and organ ANIMAL α-AMYLASES 29 FIG.

With the advent of zone electrophoresis, pol­ ymorphisms of a variety of proteins, particularly serum proteins, were described. Several of these proteins, among them the so called "thread 40 ROBERT C. KARN AND GEORGE M. MALACINSKI proteins" (Ashton, 1957), had, at the time, undetermined functions. Ashton (1957, 1958) described polymorphisms of thread proteins in cattle (Fig. 11) and pigs (Fig. 12) (Ashton, 1960). Thread protein was subsequently demonstrated to be the enzyme amylase (Ashton, 1965).

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