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Biochemical Properties in Relation to Isoenzymes

In our opinion, it is unwise to base a classification of isoenzymes solely on starch-gel electrophoresis data. For example, the work of Boyer, Chiandussi, and many others (B39, C7, M33-M36) shows a great complexity in the location of bands derived from individual organs. True, one can identify the heat-stable or -unstable zones and even those [Pg.323]

The pattern requires the division of alkaline phosphatase activity into two main parts (LPSAP and non-LPSAP) and each of these into two subgroups (heat-stable and heat-unstable moieties)  [Pg.324]

The analysis of such data obtained on normal subjects is considered basic to attempts to interpret hyperphosphatasemia in patients. [Pg.324]

Data to be presented in Sections 7.2, 8, and 9.2 were all obtained with the manual method (S49, F14). It is to be expected that these results may differ numerically to some extent from those now being collected in greater numbers with the AutoAnalyzer. Accordingly, Tables 10, 11, 12, and 14 are significant in that they provide an experimental basis for developing the concept of a biochemical pattern for serum alkaline phosphatase activity. The figures (mean SD) will no doubt require revision with the availability of AutoAnalyzer data by the method of Fishman and Green (F8). [Pg.324]

Individuals characterized by the slow-moving band in the intestinal position are invariably secretors of ABH substance according to Lang-man et al. (L2). This is the basis for dividing the normal subjects into two groups, one with the slow-moving band and the other without the slow-moving band. Some secretors with A blood type fail to exhibit the band (L2). [Pg.324]


See other pages where Biochemical Properties in Relation to Isoenzymes is mentioned: [Pg.255]    [Pg.323]   


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