Skip to main content

. 1958 Aug;69(4):573–582. doi: 10.1042/bj0690573

Studies on sulphatases. 22. The anomalous kinetics of arylsulphatase A of human tissues: interpretation of the anomalies^*

H Baum ¹, K S Dodgson ¹

PMCID: PMC1196600 PMID: 13572320

582

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

BAUM H., DODGSON K. S., SPENCER B. Studies on sulphatases. 21. The anomalous kinetics of arylsulphatase A of human tissues: the anomalies. Biochem J. 1958 Aug;69(4):567–572. doi: 10.1042/bj0690567. [DOI] [PMC free article] [PubMed] [Google Scholar]
DIXON G. H., NEURATH H. Acylation of the enzymatic site of delta-chymotrypsin by esters, acid anhydrides, and acid chlorides. J Biol Chem. 1957 Apr;225(2):1049–1059. [PubMed] [Google Scholar]
DODGSON K. S., WYNN C. H. Studies on sulphatases. 19. The purification and properties of arylsulphatase B of human liver. Biochem J. 1958 Mar;68(3):387–395. doi: 10.1042/bj0680387. [DOI] [PMC free article] [PubMed] [Google Scholar]
McDONALD C. E., BALLS A. K. Analogues of acetyl chymotrypsin. J Biol Chem. 1957 Aug;227(2):727–736. [PubMed] [Google Scholar]
ROY A. B. The kinetics of sulphatase A. Experientia. 1957 Jan 15;13(1):32–34. doi: 10.1007/BF02156950. [DOI] [PubMed] [Google Scholar]
ROY A. B. The sulphatase of ox liver. II. The purification and properties of sulphatase A. Biochem J. 1953 Nov;55(4):653–661. doi: 10.1042/bj0550653. [DOI] [PMC free article] [PubMed] [Google Scholar]

ACTIONS

RESOURCES