Biochemical evidence for membrane-bound endoderm-specific alkaline phosphatase in larvae of the ascidian, Halocynthia roretzi

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6 Citations (Scopus)

Abstract

An endoderm-specific alkaline phosphatase with a molecular mass of 86 kDa has been found in tadpole larvae of the ascidian, Halocynthia roretzi. The histochemical staining of sections of the larvae revealed that the enzyme is a membrane-associated protein. Two distinct bands were detected by zymographic technique on SDS/PAGE of the membrane preparation of the larvae. The two enzymes can be solubilized from the membrane preparation by sodium cholate and separated from each other by Cibacron blue-3GA affinity chromatography The 86-kDa enzyme is likely to be the endoderm-specific one because the susceptibilities to alkaline phosphatase inhibitors coincide between the 86-kDa enzyme and that found in the endoderm of larvae by histochemical staining. The endoderm-specific alkaline phosphatase was purified and its N-terminal amino acid sequence was found to show little similarity to those of other proteins.

Original languageEnglish
Pages (from-to)485-489
Number of pages5
JournalEuropean Journal of Biochemistry
Volume240
Issue number2
DOIs
Publication statusPublished - 1996 Jan 1
Externally publishedYes

Keywords

  • Alkaline phosphatase
  • Ascidian larvae
  • Differentiation
  • Endoderm

ASJC Scopus subject areas

  • Biochemistry

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