Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins

Biochemistry ◽  
1986 ◽  
Vol 25 (26) ◽  
pp. 8418-8425 ◽  
Author(s):  
Sentaro Kobayashi ◽  
Francine Eden-McCutchan ◽  
Paul Framson ◽  
Paul Bornstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence

scholarly journals The sequence of the mouse 14 kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes

1989 ◽  
Vol 261 (3) ◽  
pp. 847-852 ◽  
Author(s):  
T J G Wilson ◽  
M N Firth ◽  
J T Powell ◽  
F L Harrison
Keyword(s):  
Amino Acid ◽  
Basement Membrane ◽  
Amino Acid Sequence ◽  
Genomic Dna ◽  
Cdna Probe ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence ◽  
3T3 Fibroblasts ◽  
Cytoplasmic Ribosomes ◽  
Binding Lectin

The partial amino acid sequence of the mouse 14 kDa beta-galactoside-binding lectin has been deduced from cDNA clones corresponding to 86% of the coding sequence and extending to the polyadenylation signal. The deduced amino acid sequence for the murine lectin shows 94% identity with the rat, 89% with human, 86% with bovine and 46% with the chicken 14 kDa lectins. A cDNA probe has been used to analyse genomic DNA and identify a single mRNA of approx. 570 bp in 3T3 fibroblasts, murine erythroleukaemia cells and the murine basement-membrane-secreting Engelbreth-Holm-Swarm tumour. Analysis of free and bound polyribosomes has shown that the lectin message is translated on free cytoplasmic ribosomes.

Molecular studies on osmoprimed seeds of cauliflower: a partial amino acid sequence of a vigour-related protein and osmopriming-enhanced expression of putative aspartic protease

1995 ◽  
Vol 5 (3) ◽  
pp. 177-181 ◽  
Author(s):  
Yuzo Fujikura ◽  
Cees M. Karssen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Probe ◽  
Soybean Seed ◽  
Aspartic Protease ◽  
Cdna Clones ◽  
High Homology ◽  
Related Protein ◽  
Partial Amino Acid Sequence ◽  
Two Dimensional Gel Electrophoresis

AbstractA partial amino acid sequence of a vigour-related protein, V-1, from cauliflower (Brassica oleracea L.) seeds was obtained, after isolation by two-dimensional gel electrophoresis and gas-phase micro-sequencing. The sequence was found to have high homology to soybean seed maturation proteins. However, the position of the sequence in the V-1 polypeptide suggests that the V-1 and soybean proteins have different polypeptide structures. An osmoprimed seeds cDNA library was constructed and has been screened by a cDNA probe derived from the V-1 sequence. Two cDNA clones with high homology to aspartic protease (EC 3.4.23) from barley grain were isolated. The expression of putative aspartic protease mRNA was found to be enhanced by osmopriming, however the clones were found to have no significant sequence homology to the V-1.

scholarly journals The murine Fc receptor for immunoglobulin: purification, partial amino acid sequence, and isolation of cDNA clones.

1986 ◽  
Vol 83 (18) ◽  
pp. 6980-6984 ◽  
Author(s):  
M. L. Hibbs ◽  
I. D. Walker ◽  
L. Kirszbaum ◽  
G. A. Pietersz ◽  
N. J. Deacon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fc Receptor ◽  
Cdna Clones ◽  
Partial Amino Acid Sequence

Partial Amino Acid Sequence of a Cellulase-Like Component with IgE-Binding Properties from Stachybotrys chartarum

2004 ◽  
Vol 133 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Marja Kärkkäinen ◽  
Päivi Raunio ◽  
Jaakko Rautiainen ◽  
Seppo Auriola ◽  
Kaj Hinke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Stachybotrys Chartarum ◽  
Partial Amino Acid Sequence ◽  
Binding Properties ◽  
Ige Binding

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

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