By Robert B. McComb
There will be doubtless that alkaline phosphatase is among the so much greatly in vestigated of all enzymes. This has resulted from the ubiquity of its distribution, and from the benefit and sensitivity with which its task might be measured. regrettably, those wide-ranging yet frequently superficial experimental reports were up by means of in depth and systematic investigations in just a number of restricted parts of the biochemistry and chemical pathology of alkaline phosphatase. the outcome has been the buildup of a systematic literature of intimidating proportions, and the inevitable rediscovery of already identified evidence concerning the enzyme. Scientists are taught early of their careers that, within the phrases of Sir John Herschel, "Hasty generalization is the bane of technology. " however, moments arrive in all spheres of clinical job whilst generalization turns into crucial, to codify and to choose from the mass of knowledge already collected, and to supply beginning issues for brand spanking new advancements and new strains of research. this is often very true in a box equivalent to alkaline phosphatase learn, during which very genuine hazards exist that the seeds of basic realizing may be misplaced amidst an unexamined harvest of empirical observations. The historical past of the research of alkaline phosphatase presents a number of circumstances whilst worthy generalizations have emerged. sometimes, the conclusions drawn at the foundation of accessible proof have been improper; extra often, they've got stood the try of additional experimentation, and continuously, they've got supplied new insights into the character and correct ties of this enzyme.
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Additional info for Alkaline Phosphatase
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82 In cell fractions largely identified as plasma membranes, specific alkaline phosphatase and other plasma-membrane-enzyme 83 activities were 12-14 times greater than those in whole homogenates. Alkaline phosphatase activity was comparable to that found in purified membrane fractions of rat intestinal brush borders. 84 U1samer et al. 82 were not entirely satisfied tha,t the activity was of plasma-membrane origin, since on several occasions preparations contaminated with other cell fractions gave higher activities than apparently "pure" plasma-membrane fractions.
Chemical nature of the cophosphomonoesterase, Enzymologia, 15,154,1951. 87. Alvarez, E. , Purification of kidney alkaline phosphatase, Biochem. , 69,312,1958. 88. , Reversible Abspaltung des zweiten Metalles der alkalischen Phosphatase. II, Biochern. ,308, 37,1941. 89. , and Porteous, J. , The metal ion activation of the alkaline beta glycerophosphatase of rabbit small intestine, Biochern. , 95, 475, 1965. 90. Plocke, D. , Alkaline phosphatase of Escherichia coli: A zinc metalloenzyme, Biochemistry, 1,373,1962.