Baum, H. published the artcileSulfatases. XXI. The anomalous kinetics of arylsulfatase A of human tissues: the anomalies, Synthetic Route of 6217-68-1, the publication is Biochemical Journal (1958), 567-72, database is CAplus and MEDLINE.
cf. C.A. 52, 14725h. Preparations of human arylsulfatase A exhibit anomalous time-activity curves when incubated with di-K 2-hydroxy-5-nitrophenylsulfate (I), K p-acetylphenylsulfate, and K p-nitrophenyl sulfate. The rate of the reaction increases with time, at a rate which varies with the enzyme concentration The rate is proportional to some value greater than the 1st power of the enzyme concentration, depending upon the length of incubation time. Increasing substrate concentration during the initial period of incubation results in an increase in the rate to a maximum, whereas with prolonged incubation with the substrate the rate passes through a maximum and falls at higher substrate concentrations During the early incubation period there are optima at pH 4.4 and 5.0, whereas as the period of incubation is extended the 2 peaks merge at pH 4.4, and then shift to 4.7. The time-activity curves obtained at 20.5 and 30.5° cross those obtained at 37.5 and 50.5°; this indicates that enzyme destruction is not an important factor. The anomalous kinetics appear to be a feature peculiar to mammalian arylsulfatase A and are not shown by human arylsulfatase B or the arylsulfatases of limpets (Patella vulgata), Alcaligenes metalcaligenes, Taka-Diastase, and Helix pomatia.
Biochemical Journal published new progress about 6217-68-1. 6217-68-1 belongs to esters-buliding-blocks, auxiliary class Salt,Nitro Compound,Sulfonate,Benzene, name is Potassium 4-nitrophenyl sulfate, and the molecular formula is C6H4KNO6S, Synthetic Route of 6217-68-1.
Referemce:
https://en.wikipedia.org/wiki/Ester,
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