scholarly journals Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein

1989 ◽  
Vol 259 (1) ◽  
pp. 283-290 ◽  
Author(s):  
W M Abbott ◽  
A Mellor ◽  
Y Edwards ◽  
T Feizi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Cdna Library ◽  
Basic Protein ◽  
Cdna Clones ◽  
Antigenic Relationship ◽  
Lectin Protein ◽  
Binding Lectin ◽  
Major Domain

A full-length cDNA clone for the 13-14 kDa soluble beta-galactoside-binding lectin was isolated from a bovine fibroblast cDNA library. The derived amino acid sequence shows eight differences from a preliminary partial amino acid sequence given previously for the bovine heart lectin. This observation led to a re-examination of the data and correction of the heart lectin protein sequence. Except for a possible polymorphism of the heart lectin at position 57, the fibroblast and heart lectin sequences are considered identical. The epitope recognized by two monoclonal anti-(bovine lectin) antibodies, 36/8 and 9/5, was identified as the tetrapeptide sequence W-G-A/S-E/D by the isolation of several different cDNA clones from a human intestine cDNA library. A similar tetrapeptide is present in all of the soluble beta-galactoside-binding animal lectins sequenced thus far. It is also found in myelin basic protein, which we show is antigenically cross-reactive with the lectin. In myelin basic protein the tetrapeptide is a part of the major domain previously shown to be responsible for the induction of experimental allergic encephalomyelitis.

Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self-Association

1990 ◽  
Vol 55 (3) ◽  
pp. 950-955 ◽  
Author(s):  
Trudy J. Milne ◽  
Annette R. Atkins ◽  
Juanita A. Warren ◽  
Wendy P. Auton ◽  
Ross Smith
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Amino Acid ◽  
Protein Amino Acid Sequence ◽  
Self Association

scholarly journals Cloning and sequencing of protochlorophyllide reductase

1990 ◽  
Vol 265 (3) ◽  
pp. 789-798 ◽  
Author(s):  
P M Darrah ◽  
S A Kay ◽  
G R Teakle ◽  
W T Griffiths
Keyword(s):  
Amino Acid ◽  
Chemical Analysis ◽  
Amino Acid Sequence ◽  
Cdna Library ◽  
Avena Sativa ◽  
Cdna Clones ◽  
Lambda Phage ◽  
Cloning And Sequencing ◽  
Protochlorophyllide Reductase ◽  
Cnbr Cleavage

Putative protochlorophyllide reductase cDNA clones (252 and 113) were isolated from an etiolated-oat (Avena sativa) cDNA library. These were used to indirectly characterize a further clone, p127, isolated from a lambda-phage gt11 cDNA library. The latter (1.15 kb in length) was sequenced, and the derived amino acid sequence was shown to be remarkably similar to that derived from chemical analysis of a CNBr-cleavage fragment of the purified reductase, p127 codes for more than 95% of the reductase protein.

Amino Acid Sequence of Porcine Myelin Basic Protein

1985 ◽  
Vol 44 (1) ◽  
pp. 134-142 ◽  
Author(s):  
Jun-ichi Kira ◽  
Gladys E. Deibler ◽  
Henry C. Krutzsch ◽  
Russell E. Martenson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein

scholarly journals The binding of calmodulin to myelin basic protein and histone H2B

1980 ◽  
Vol 189 (2) ◽  
pp. 227-240 ◽  
Author(s):  
R J Grand ◽  
S V Perry
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Binding Protein ◽  
Bovine Brain ◽  
Sequence Determination ◽  
Partial Amino Acid Sequence ◽  
Histone H2b ◽  
Calmodulin Binding

1. A calmodulin-binding protein of apparent mol.wt. 19 000 has been purified from chicken gizzard. Similar proteins have been isolated from bovine uterus, rabbit skeletal muscle and rabbit liver. 2. These proteins migrated as an equimolar complex with bovine brain calmodulin on electroporesis on polyacrylamide gels in the presence of Ca2+ and 6M-urea. The complex was dissociated in the presence of EGTA. 2. The chicken gizzard calmodulin-binding protein has been shown to be identical with chicken erythrocyte histone H2B on the basis of partial amino acid sequence determination. 4. The calmodulin-binding proteins of apparent mol.wt. 22 000 isolated previously from bovine brain [Grand & Perry (1979) Biochem. J. 183, 285-295] has been shown, on the basis of partial amino-acid-sequence determination, to be identical with myelin basic protein. 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B). 6. The phosphorylation of myelin basic protein by phosphorylase kinase is partially inhibited, whereas the phosphorylation of uterus calmodulin-binding protein (histone H2B) is unaffected by calmodulin or troponin C. 7. The subcellular distribution of myelin basic protein and calmodulin suggests that the two proteins do not exist as a complex in vivo.

scholarly journals Amino acid sequence conservation of the algesic fragment of myelin basic protein is required for its interaction with CDK 5 and function in pain

FEBS Journal ◽  
2018 ◽  
Vol 285 (18) ◽  
pp. 3485-3502
Author(s):  
Andrei V. Chernov ◽  
Albert G. Remacle ◽  
Swathi K. Hullugundi ◽  
Piotr Cieplak ◽  
Mila Angert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Sequence Conservation ◽  
And Function ◽  
Amino Acid Sequence Conservation

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.

scholarly journals Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.

1988 ◽  
Vol 263 (25) ◽  
pp. 12559-12563
Author(s):  
T L Wasmoen ◽  
M P Bell ◽  
D A Loegering ◽  
G J Gleich ◽  
F G Prendergast ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Amino Acid Sequence Analysis ◽  
Human Eosinophil ◽  
Eosinophil Granule
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