By Robert B. McComb
There might be without doubt that alkaline phosphatase is among the such a lot commonly in vestigated of all enzymes. This has resulted from the ubiquity of its distribution, and from the convenience and sensitivity with which its task will be measured. regrettably, those wide-ranging yet frequently superficial experimental experiences were up by way of extensive and systematic investigations in just a number of restricted components of the biochemistry and chemical pathology of alkaline phosphatase. the end result 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 medical task whilst generalization turns into crucial, to codify and to choose between the mass of knowledge already collected, and to supply beginning issues for brand spanking new advancements and new strains of research. this can be very true in a box equivalent to alkaline phosphatase learn, within which very actual hazards exist that the seeds of primary figuring out could be misplaced amidst an unexamined harvest of empirical observations. The historical past of the research of alkaline phosphatase presents a number of cases whilst important generalizations have emerged. sometimes, the conclusions drawn at the foundation of obtainable facts have been improper; extra usually, they've got stood the try out of extra experimentation, and regularly, they've got supplied new insights into the character and correct ties of this enzyme.
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Extra info for Alkaline Phosphatase
61. Kay, H. , Kidney phosphatase,Biochem. , 20,791,1926. 62. Cattell, J. M. and Cattell, J. ), American Men of Science, A Biographical Directory, The Science Press, New York, 1933. 63. Kay, H. , The phosphatases of mammalian tissues, Biochem. , 22, 855, 1928. 64. , Uber die Nierenphosphatase. I. Mitteilung zur Kenntnis der Phosphatasen,z. Physiol. , 232, 165, 1935. 65. , Uber eine einfache Methode zur Darstellung hochaktiver Phosphatasepraparate aus tierischem Material, Z. Physiol. , 232,189,1935.
King, E. , and Armstrong, A. , A convenient method for determining serum and bile phosphatase activity, Can. Med. Assoc. , 31, 376, 1934. 60. Obituary notice, Robert Robison (1883-1941), Biochem. , 35, 1081, 1941. 61. Kay, H. , Kidney phosphatase,Biochem. , 20,791,1926. 62. Cattell, J. M. and Cattell, J. ), American Men of Science, A Biographical Directory, The Science Press, New York, 1933. 63. Kay, H. , The phosphatases of mammalian tissues, Biochem. , 22, 855, 1928. 64. , Uber die Nierenphosphatase.
Thus, glutaraldehyde-flXed E. 48 In Pseudomonas aernginosa, glutaraldehyde fIxation caused the enzyme to appear on the cell surface. 52 Wetzel et al. 48 showed that alkaline phosphatase activity in E. coli is particularly intense at the polar caps of these elongated organisms. Some bacteria, such as certain mutants of Bacillus subtilis 53 and E. coli ,54 have defective cell walls. These organisms release alkaline phosphatase into the culture medium during growth. In some instances, as in Bacteroides rnminicola, the enzyme is fIrmly bound to the cell-wall structures and cannot be released except by complete disruption of the cells.