scholarly journals Amino acid sequence of the vitronectin receptor alpha subunit and comparative expression of adhesion receptor mRNAs.

1987 ◽  
Vol 262 (29) ◽  
pp. 14080-14085 ◽  
Author(s):  
S Suzuki ◽  
W S Argraves ◽  
H Arai ◽  
L R Languino ◽  
M D Pierschbacher ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alpha Subunit ◽  
Vitronectin Receptor ◽  
Adhesion Receptor ◽  
Receptor Alpha ◽  
Receptor Mrnas

scholarly journals Amino acid sequence of the human fibronectin receptor.

1987 ◽  
Vol 105 (3) ◽  
pp. 1183-1190 ◽  
Author(s):  
W S Argraves ◽  
S Suzuki ◽  
H Arai ◽  
K Thompson ◽  
M D Pierschbacher ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Receptor Subunit ◽  
Fibronectin Receptor ◽  
Adhesion Receptor ◽  
Receptor Beta

The amino acid sequence deduced from cDNA of the human placental fibronectin receptor is reported. The receptor is composed of two subunits: an alpha subunit of 1,008 amino acids which is processed into two polypeptides disulfide bonded to one another, and a beta subunit of 778 amino acids. Each subunit has near its COOH terminus a hydrophobic segment. This and other sequence features suggest a structure for the receptor in which the hydrophobic segments serve as transmembrane domains anchoring each subunit to the membrane and dividing each into a large ectodomain and a short cytoplasmic domain. The alpha subunit ectodomain has five sequence elements homologous to consensus Ca2+-binding sites of several calcium-binding proteins, and the beta subunit contains a fourfold repeat strikingly rich in cysteine. The alpha subunit sequence is 46% homologous to the alpha subunit of the vitronectin receptor. The beta subunit is 44% homologous to the human platelet adhesion receptor subunit IIIa and 47% homologous to a leukocyte adhesion receptor beta subunit. The high degree of homology (85%) of the beta subunit with one of the polypeptides of a chicken adhesion receptor complex referred to as integrin complex strongly suggests that the latter polypeptide is the chicken homologue of the fibronectin receptor beta subunit. These receptor subunit homologies define a superfamily of adhesion receptors. The availability of the entire protein sequence for the fibronectin receptor will facilitate studies on the functions of these receptors.

scholarly journals Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit.

1990 ◽  
Vol 265 (8) ◽  
pp. 4204-4209
Author(s):  
K Schott ◽  
J Kellermann ◽  
F Lottspeich ◽  
A Bacher
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alpha Subunit

scholarly journals The complete Amino Acid Sequence of the major alpha subunit of the Lectin from the seeds of Dioclea grandiflora (Mart.)

1984 ◽  
Vol 144 (1) ◽  
pp. 107-111
Author(s):  
M. Richardson ◽  
F. D. A. P. Campos ◽  
R. M. Moreira ◽  
I. L. Ainouz ◽  
R. Begbie ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alpha Subunit ◽  
Complete Amino Acid Sequence ◽  
Dioclea Grandiflora

scholarly journals The complete amino acid sequence of the major alpha subunit of the lectin from the seeds of Dioclea grandiflora (Mart)

1984 ◽  
Vol 144 (1) ◽  
pp. 101-111 ◽  
Author(s):  
Michael RICHARDSON ◽  
Francisco D. A. P. CAMPOS ◽  
Renato A. MOREIRA ◽  
Iracaema L. AINOUZ ◽  
Robert BEGBIE ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alpha Subunit ◽  
Complete Amino Acid Sequence ◽  
Dioclea Grandiflora

Complementary DNA and derived amino acid sequence of the .alpha. subunit of human complement protein C8: evidence for the existence of a separate .alpha. subunit messenger RNA

Biochemistry ◽  
1987 ◽  
Vol 26 (12) ◽  
pp. 3556-3564 ◽  
Author(s):  
A. Gururaj Rao ◽  
O. M. Zack Howard ◽  
Simon C. Ng ◽  
Alexander S. Whitehead ◽  
Harvey R. Colten ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Messenger Rna ◽  
Alpha Subunit ◽  
Human Complement ◽  
Complement Protein ◽  
Complementary Dna ◽  
Complement Protein C8

Isolation, sequencing, and disruption of the CKA1 gene encoding the alpha subunit of yeast casein kinase II

1988 ◽  
Vol 8 (11) ◽  
pp. 4981-4990
Author(s):  
J L Chen-Wu ◽  
R Padmanabha ◽  
C V Glover
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Product ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Protein Sequencing ◽  
Alpha Subunit ◽  
Yeast Genome ◽  
Gene Encoding ◽  
Alpha Gene

Casein kinase II of Saccharomyces cerevisiae contains two distinct catalytic subunits, alpha and alpha', which must be encoded by separate genes (R. Padmanabha and C. V. C. Glover, J. Biol. Chem. 262:1829-1835, 1987). The gene encoding the 42-kilodalton alpha subunit has been isolated by screening a yeast genomic library with oligonucleotide probes synthesized on the basis of the N-terminal amino acid sequence of the polypeptide. This gene (designated CKA1) contains an intron-free open reading frame of 372 amino acid residues. The deduced amino acid sequence is 67% identical to the alpha subunit of Drosophila melanogaster casein kinase II. The CKA1 gene product appears to be distantly related to other known protein kinases but exhibits highest similarity to the CDC28 gene product and its homolog in other species. Gene replacement techniques have been used to generate a null cka1 mutant allele. Haploid and diploid strains lacking a functional CKA1 gene appear to be phenotypically wild type, presumably because of the presence of the alpha' gene. Interestingly, the CKA1 gene appears to be single copy in the yeast genome; i.e., the alpha' gene, whose existence is known from biochemical studies and protein sequencing, cannot be detected by low-stringency hybridization.

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