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Human platelet as an independent unit for sulfate conjugation

Journal Article · · Life Sci.; (United States)

The human platelets possess a full complement of enzymes capable of synthesizing N-acetyldopamine (NADA) /sup 35/sulfate from ATP, Mg/sup + +/ and sodium /sup 35/sulfate. The pH optimum for this three-step overall sulfate conjugation (comprising of the ATP sulfurylase, APS kinase and phenolsulfotransferase reactions) is 8.6 and the reactions proceeded progressively for several hours. Both ATP and Mg/sup + +/ ions, above their respective optimal concentrations of 5 and 7 mM, inhibited the sulfate conjugation of NADA. The apparent Km values for NADA as determined by the phenolsulfotransferase (PST) and overall reactions were similar in magnitude being 2.6 and 4.8 ..mu..M, respectively, while that for sodium /sup 35/sulfate was 202 ..mu..M. A comparison of these two activities in 62 platelet preparations of normal subjects showed that the rate of the PST reaction was generally higher than the overall reaction even though the PST assay was carried out at suboptimal concentration of PAPS. There was a positive correlation (r=0.82) between the two sets of data, suggesting that the PST reaction probably has some control over the rate of overall sulfate conjugation.

Research Organization:
National Univ., Singapore
OSTI ID:
5481533
Journal Information:
Life Sci.; (United States), Journal Name: Life Sci.; (United States) Vol. 42:11; ISSN LIFSA
Country of Publication:
United States
Language:
English