Isolation and Characterization of a D-Galactose-binding Lectin from the Acorn Barnacle <i>Balanus rostratus</i>
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- Toda Michitoshi
- Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
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- Jimbo Mitsuru
- Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
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- Muramoto Koji
- Graduate School of Agriculture, Department of Biological Resource Sciences, Tohoku University
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- Sakai Rvuichi
- Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
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- Kamiya Hisao
- Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
Bibliographic Information
- Other Title
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- Isolation and Characterization of a D-Galactose-binding Lectin from the Acorn Barnacle Balanus rostratus
- Isolation and Characterization of a D G
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Abstract
The hemolymph of the acorn barnacle Balanus rostratus showed hemagglutinating activity and inhibition of calcium carbonate crystallization. A lectin having D-galactose-binding specificity was isolated from the hemolymph by a combination of affinity chromatography on acid-treated agarose gel and HPLC. The purified lectin was dependent on the presence of calcium ion for hemagglutinating activity. In SDS-PAGE, it gave one protein band (25kDa) under a reduced condition, while it gave two components (35 and 95kDa) without a reducing agent. The molecular mass of the intact lectin was estimated to be 120kDa by HPLC on TSK G-3000SW. Isolectric point was determined to be pH 4.4. The same amino-terminal sequence, Tyr-Val-Ser-Asn-Gln-Ser-Val-Glu-Pro-Asp-Ser-Ala-Asp-Thr-Ala, was obtained with the purified lectin as well as the components observed in SDS-PAGE. The purified lectin did not inhibit calcium carbonate crystallization at 1mg/30ml, although the hemolymph inhibited the crystallization at 0.1mg protein/30ml. The inhibitory factor(s) was an acidic and small molecular-weight compound(s).
Journal
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- Fisheries science
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Fisheries science 64 (4), 638-642, 1998
The Japanese Society of Fisheries Science
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Details
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- CRID
- 1390001204428065024
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- NII Article ID
- 130003903215
- 10004875638
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- NII Book ID
- AA10993718
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- NDL BIB ID
- 4547687
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- ISSN
- 09199268
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed