N.M.R. Studies of Myelin Basic Protein. III. Interactions of the Protein with Lipid Micelles by 1H and 31P N.M.R.

1979 ◽  
Vol 32 (12) ◽  
pp. 2631 ◽  
Author(s):  
LAT Littlemore ◽  
RW Ledeen
Keyword(s):  
Myelin Basic Protein ◽  
Conformational Changes ◽  
Basic Protein ◽  
Polypeptide Chain ◽  
Lipid Binding ◽  
Bovine Brain ◽  
Gm1 Ganglioside ◽  
Spectral Changes ◽  
Central Regions ◽  
Lipid Micelles

The interactions of bovine myelin basic protein with bovine brain GM1 ganglioside and with lysophosphatidylcholine have been followed by 1H and 31P N.M.R. The effect of the binding of lipid on the protein spectrum could be followed in methyl peaks due to methionine and NG-methylarginine and in peaks from aromatic side chains. Both lipids caused broadening of methyl resonances from methionine-20, the unique NG-methylarginine and phenylalanines. The N.M.R. spectral changes on interaction of peptides derived from N-terminal and C-terminal halves of the protein with lysolecithin indicated that the lipid binding was associated with conformational changes involving the central regions of the polypeptide chain and the methylarginine residue. The 31P spectra suggest that the average phosphate group in lysophosphatidylcholine becomes more mobile as a result of binding of basic protein to the lipid micelle.

MYELIN BASIC PROTEIN IN FROZEN AND UNFROZEN BOVINE BRAIN: A STUDY OF AUTOLYTIC CHANGES IN SITU

1975 ◽  
Vol 25 (3) ◽  
pp. 193-195 ◽  
Author(s):  
K. A. Ansari ◽  
H. Hendrickson ◽  
A. A. Sinha ◽  
A. Rand
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Bovine Brain

N.M.R. studies on myelin basic protein. I. 13C spectra in aqueous solutions

1978 ◽  
Vol 31 (11) ◽  
pp. 2367 ◽  
Author(s):  
BE Chapman ◽  
WJ Moore
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Polypeptide Chain ◽  
Random Coil ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Native Protein ◽  
Denatured Protein ◽  
Coil Structure ◽  
Random Coil Structure

Carbon-13 n.m.r, spectra have been obtained for bovine myelin basic protein at pD 4.4 in D2O and in 6 M guanidine deuterochloride solutions. Chemical-shift differences between resonances from some amino acid residues are interpreted in terms of structured regions in the polypeptide chain of the native protein, whereas the denatured protein displays the spectrum expected for an essentially random coil. Measurements of T1 and n.O.e. provide quantitative data on the dynamics of the backbone and side-chain carbons, and give support to the conclusion that the native protein does not have a random-coil structure.

scholarly journals Purification and kinetic mechanism of S-adenosylmethionine: myelin basic protein methyltransferase from bovine brain

1988 ◽  
Vol 250 (1) ◽  
pp. 221-226 ◽  
Author(s):  
P R Young ◽  
C M Waickus
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
High Specificity ◽  
Kinetic Mechanism ◽  
Bovine Brain ◽  
Tryptic Cleavage ◽  
Protein Methyltransferase

The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant. The purification involves acid-base and (NH4)2SO4 precipitation, chromatography over Sephadex G-100 and DEAE-cellulose, followed by preparative isoelectric focusing. The enzyme has a pI of 5.60 +/- 0.05, and the Mr is estimated to be between 71,000 (from SDS/polyacrylamide-gel electrophoresis) and 74,500 (from gel filtration). The enzyme is stable at 37 degrees C for over 2 h, is stable frozen and does not require metal ions or reductants. The enzyme shows a high specificity for MBP and does not accept polyarginine as a substrate; F1 histone is methylated at 37% of the rate of MBP. Methylation occurs on an arginine residue in a single h.p.l.c.-resolvable peptide from the tryptic cleavage of MBP. Simple saturation kinetics are observed with respect to both substrates, with Km values of 18 microM and 32 microM for MBP and AdoMet respectively. The simplest kinetic mechanism that is consistent with the data requires ordered rapid-equilibrium binding, with AdoMet as the first substrate. The enzyme isolated in this work is different, both physically and kinetically, from the histone-specific arginine methyltransferases described by other workers. A new, simple, assay system for the methylation of MBP is described.

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.

Evidence for Specific Polypeptide Chain Folding in Myelin Basic Protein from Reactions Between Fragments of the Protein and Monoclonal Antibodies

2006 ◽  
Vol 47 (3) ◽  
pp. 764-771 ◽  
Author(s):  
Ellsworth C. Alvord ◽  
Sarka Hruby ◽  
Russell E. Martenson ◽  
Gladys E. Deibler ◽  
Mona J. Law
Keyword(s):  
Monoclonal Antibodies ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Polypeptide Chain ◽  
Chain Folding
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