Arylsulfatase B of human lung. Isolation, characterization, and interaction with slow-reacting substance of anaphylaxis

Arylsulfatase B was separated from arylsulfatase A in extracts of human lung tissue by anion exchange chromatography and further purified by gel filtration and cation exchange chromatography. Arylsulfatase B of human lung was similar to that enzyme in other tissues and species, exhibiting an apparent mol wt of approximately 60,000, a pH optimum for cleavage of 4-nitrocatechol sulfate (pNCS) of 5.5-6.0, and a sensitivity to inhibition by phosphate ions and especially pyrophosphate in the presence of NaCl. Human lung arylsulfatase B inactivated slow-reacting substance of anaphylaxix (SRS-A) in a linear time-dependent reaction in which the rate was determined by the enzyme-to-substrate ratio. Cleavage of pNCS by human lung arylsulfatase B was competitively suppressed by SRS-A. The finding that human lung tissue contains predominately arylsulfatase B discloses a potential regulatory mechanism for inactivation of SRS-A at or near the site of its generation.

Medienart:

Artikel

Erscheinungsjahr:

1976

Erschienen:

1976

Enthalten in:

Zur Gesamtaufnahme - volume:57

Enthalten in:

The Journal of clinical investigation - 57(1976), 3 vom: 18. März, Seite 738-44

Sprache:

Englisch

Beteiligte Personen:

Wasserman, S I [VerfasserIn]
Austen, K F [VerfasserIn]

Themen:

Chondro-4-Sulfatase
EC 3.1.6.-
EC 3.1.6.9
Journal Article
Research Support, U.S. Gov't, P.H.S.
SRS-A
Sulfatases

Anmerkungen:

Date Completed 29.04.1976

Date Revised 13.11.2018

published: Print

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM00003133X