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 |
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Erscheinungsjahr: |
1976 |
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Erschienen: |
1976 |
Enthalten in: |
Zur Gesamtaufnahme - volume:57 |
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Enthalten in: |
The Journal of clinical investigation - 57(1976), 3 vom: 18. März, Seite 738-44 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Wasserman, S I [VerfasserIn] |
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Themen: |
Chondro-4-Sulfatase |
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Anmerkungen: |
Date Completed 29.04.1976 Date Revised 13.11.2018 published: Print Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM00003133X |
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100 | 1 | |a Wasserman, S I |e verfasserin |4 aut | |
245 | 1 | 0 | |a Arylsulfatase B of human lung. Isolation, characterization, and interaction with slow-reacting substance of anaphylaxis |
264 | 1 | |c 1976 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
338 | |a Band |b nc |2 rdacarrier | ||
500 | |a Date Completed 29.04.1976 | ||
500 | |a Date Revised 13.11.2018 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a 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 | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
650 | 7 | |a SRS-A |2 NLM | |
650 | 7 | |a Sulfatases |2 NLM | |
650 | 7 | |a EC 3.1.6.- |2 NLM | |
650 | 7 | |a Chondro-4-Sulfatase |2 NLM | |
650 | 7 | |a EC 3.1.6.9 |2 NLM | |
700 | 1 | |a Austen, K F |e verfasserin |4 aut | |
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