The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa

Koji Muramoto; Hisao Kamiya

doi:10.1016/0167-4838(86)90027-0

The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa

Koji Muramoto, Hisao Kamiya

Research output: Contribution to journal › Article › peer-review

59 Citations (Scopus)

Abstract

The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (M_r 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG₁. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.

Original language	English
Pages (from-to)	285-295
Number of pages	11
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	874
Issue number	3
DOIs	https://doi.org/10.1016/0167-4838(86)90027-0
Publication status	Published - 1986 Dec 12
Externally published	Yes

Keywords

(Acorn barnacle)
Agglutinin
Amino-acid sequence
Invertebrate lectin
Lectin
Primary structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology

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10.1016/0167-4838(86)90027-0

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title = "The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa",

abstract = "The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG1. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.",

keywords = "(Acorn barnacle), Agglutinin, Amino-acid sequence, Invertebrate lectin, Lectin, Primary structure",

author = "Koji Muramoto and Hisao Kamiya",

note = "Funding Information: This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.",

year = "1986",

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doi = "10.1016/0167-4838(86)90027-0",

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T1 - The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa

AU - Muramoto, Koji

AU - Kamiya, Hisao

N1 - Funding Information: This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.

PY - 1986/12/12

Y1 - 1986/12/12

N2 - The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG1. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.

AB - The complete amino-acid sequence of a lectin isolated from the coelomic fluid of the acorn barnacle Megabalanus rosa has been determined. The lectin (Mr 64 000) is composed of four identical subunits of 138 amino acids. The amino-acid sequence and the location of two interchain and three intrachain disulfide bridges of the subunit were determined by the manual sequencing of peptides derived from the protein by digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 proteinase, as well as fragments produced by cleavage with cyanogen bromide. The Cys-Pro-Pro-Cys sequence at the interchain disulfide bridges was the same as that of the hinge region of human immunoglobulin IgG1. The amino acid sequence of M. rosa lectin includes some regions homologous to those in Sarcophaga (flesh fly) lectin.

KW - (Acorn barnacle)

KW - Agglutinin

KW - Amino-acid sequence

KW - Invertebrate lectin

KW - Lectin

KW - Primary structure

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DO - 10.1016/0167-4838(86)90027-0

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VL - 874

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EP - 295

JO - BBA - Protein Structure

JF - BBA - Protein Structure

SN - 1570-9639

IS - 3

ER -

The amino-acid sequence of a lectin of the acorn barnacle Megabalanus rosa

Abstract

Keywords

ASJC Scopus subject areas

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