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Cloning and sequence analysis of theMaackia amurensis haemagglutinin cDNA (1994)

Yamamoto, Kazuo ; Ishida, Chizu ; Saito, Mitsue ; [et al.]

Springer

Glycoconjugate journal 11 (1994), S. 572-575

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ISSN: 1573-4986

Keywords: Maackia amurensis haemagglutinin ; cDNA cloning, amino acid sequence ; carbohydrate recognition

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Maackia amurensis haemagglutinin (MAH) is a leguminous lectin which preferentially binds to a cluster of sialylatedO-linked carbohydrate chains (Konami Y, Yamamoto K, Osawa T, Irimura T (1994)FEBS Lett 342:334–38). In the present study a 950 bp cDNA clone encoding MAH was isolated from a cDNA library constructed from germinatedMaackia amurensis seeds. From the nucleotide sequence, MAH was predicted to consist of 285 amino acid residues containing a signal peptide of 29 amino acids. The results also confirmed our previous findings from the amino acid sequence analysis, which indicated that two highly conserved amino acid residues in all other well-known leguminous lectins were replaced in MAH. These residues were lysine-105 and aspartic acid-135. The corresponding amino acid residues in other leguminous lectins were glycine and asparagine, respectively. These differences were due to the presence of nucleotides AAA and GAT in place of AAT/C and GGA/T.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00731308

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cDNA cloning of mouse VLA-3 α subunit (1995)

Takeuchi, Ken-Ichi ; Hirano, Kazuya ; Tsuji, Tsutomu ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 57 (1995), S. 371-377

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ISSN: 0730-2312

Keywords: integrin ; VLA (very late antigen) ; adhesion molecule ; cDNA cloning ; tissue distribution ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: cDNA clones for mouse VLA (very late antigen)-3 α subunit (α3 integrin) were isolated and sequenced. The encoded mouse α3 integrin subunit was composed of 1,053 amino acid residues. The results of sequence analysis revealed similar structural characteristics to other VLA α subunits. For example, the presence of a large extracellular domain including three putative metal binding sequences, a transmembrane domain, and a short cytoplasmic domain. A higher level of its message was detected in thymus than in kidney, stomach, spleen, liver, brain, or lung by Northern blotting analysis.

Additional Material: 5 Ill.