Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

The relationship between different forms of human alpha-mannosidase

Författare

  • Alan Chester
  • A Lundblad
  • P K Masson

Summary, in English

The tissue distribution and some properties of human alpha-mannosidase (alpha-D-mannoside mannohydrolase EC 3.2.1.24) have been studied. The acidic forms of the enzyme were fairly stable, whereas the neutral forms easily lost enzymic activity. The acidic forms were sensitive to neuraminidase but the neutral forms were unaffected. The experiments indicate that the acidic components are closely related to each other, differing only in sialic acid content and possibly conformation. The neutral forms of the enzyme are probably quite different from the acidic forms both in structure and cellular function.

Publiceringsår

1975

Språk

Engelska

Sidor

341-348

Publikation/Tidskrift/Serie

Biochimica et Biophysica Acta

Volym

391

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

Elsevier

Ämne

  • Biological Sciences

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0006-3002