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 language | English |
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Pages (from-to) | 485-489 |
Number of pages | 5 |
Journal | European Journal of Biochemistry |
Volume | 240 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1996 Jan 1 |
Externally published | Yes |
Keywords
- Alkaline phosphatase
- Ascidian larvae
- Differentiation
- Endoderm
ASJC Scopus subject areas
- Biochemistry