+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Comparative activity of arylsulphatases A and B on two synthetic substrates

Comparative activity of arylsulphatases A and B on two synthetic substrates

Biochemical Journal 157(2): 353-356

Rat liver and human skin fibroblasts arylsulphatase A and B activities on both 4-methylumbelliferyl sulphate and 4-nitrocatechol sulphate were compared. The intracellular distribution of activity differed markedly when 4-methylumbelliferyl sulphate was used from that observed with 4-nitrocatechol sulphate. No discrimination between control and metachromatic leucodystrophy or mucopolysaccharidosis (type VI) could be achieved when 4-methylumbelliferyl sulphate was used as substrate. These results contrast sharply with those obtained with 4-nitrocatechol sulphate and cast doubt on the validity of 4-methylumbelliferyl sulphate as substrate for the determination of arylsulphatase A and B activities.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 039614466

Download citation: RISBibTeXText

PMID: 962873

DOI: 10.1042/bj1570353

Related references

Comparative activity of sulphatases in human liver on two synthetic substrates. Clinica Chimica Acta; International Journal of Clinical Chemistry 80(3): 423-429, 1977

Comparative activity of sulfatases ec in human liver on 2 synthetic substrates. Clinica Chimica Acta 80(3): 423-430, 1977

Comparative studies on the growth of isolated carrot tissue on part by synthetic substrates aud on a new fully synthetic medium. Flora Allig Bot Zeitung [jena] 152(3): 447-457, 1962

A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases. Biochemical Journal 288: 539-544, 1992

Arylsulphatases in human brain: separation, purification, and certain properties of the two soluble arylsulphatases. Journal of Neurochemistry 18(2): 245-257, 1971

Comparative kinetic behaviour of thrombin, plasmin and trypsin toward synthetic substrates. Nature 182(4633): 461-462, 1958

Comparative studies on arylsulphatases from fowl testes and seminal plasma. Folia Biologica 34(1): 55-72, 1986

Comparative activities of amino acid and polypeptide inhibitors on natural and synthetic substrates. Annals of the new York Academy of Sciences 146(2): 659-672, 1968

Comparative enzymatic studies of human renin acting on pure natural or synthetic substrates. Biochimica et Biophysica Acta 913(1): 10-19, 1987

Determination of trypsin activity using synthetic substrates. Sbornik Vysoke Skoly Zemedelske v Praze, Fakulta Agronomicka, B (45): 17-25, 1986

Comparative studies on the activities of collagenases from Grimontia hollisae and Clostridium hystoliticum in the hydrolysis of synthetic substrates. Journal of Biochemistry 163(5): 425-431, 2018

Diurnal changes in the activity of arylsulphatases A and B of rat liver. Folia Biologica 36(3-4): 173-182, 1988

Monitoring metalloproteinase activity using synthetic fluorogenic substrates. Current Protocols in Protein Science Chapter 21: Unit 21.16, 2004

Use of synthetic substrates for the study of the enzymatic activity of microorganisms. Comptes Rendus Hebdomadaires des Seances de l'Academie des Sciences. Serie D: Sciences Naturelles 264(2): 415-417, 1967

The activity of Clostridium histolyticum proteinase on synthetic substrates. Archives of Biochemistry and Biophysics 42(2): 327-336, 1953