scholarly journals Bovine brain creatine phosphotransferase: amino acid sequence around the essential thiol groups

1970 ◽  
Vol 117 (2) ◽  
pp. 30P-31P ◽  
Author(s):  
R S Atherton ◽  
J F Laws ◽  
B J Miles ◽  
A R Thomson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bovine Brain ◽  
Thiol Groups

Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein

1991 ◽  
Vol 11 (5) ◽  
pp. 2873-2880
Author(s):  
K Kaibuchi ◽  
T Mizuno ◽  
H Fujioka ◽  
T Yamamoto ◽  
K Kishi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Reaction ◽  
Binding Proteins ◽  
Bovine Brain ◽  
Rat Tissues ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Ras P21 ◽  
Exchange Protein

We have recently purified to near homogeneity the stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like GTP-binding proteins) from bovine brain cytosol. This regulatory protein, named GDP dissociation stimulator (GDS), stimulates the GDP/GTP exchange reaction of smg p21s by stimulating the dissociation of GDP from and the subsequent binding of GTP to them. In this study, we have isolated and sequenced the cDNA of smg p21 GDS from a bovine brain cDNA library by using an oligonucleotide probe designed from the partial amino acid sequence of the purified smg p21 GDS. The cDNA has an open reading frame encoding a protein of 558 amino acids with a calculated Mr value of 61,066, similar to the Mr of 53,000 estimated for the purified smg p21 GDS by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sucrose density gradient ultracentrifugation. The isolated cDNA is expressed in Escherichia coli, and the encoded protein exhibits smg p21 GDS activity. smg p21 GDS is overall hydrophilic, but there are several short hydrophobic regions. The smg p21 GDS mRNA is present in bovine brain and various rat tissues. smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi.

scholarly journals The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes

1974 ◽  
Vol 143 (1) ◽  
pp. 171-179 ◽  
Author(s):  
Buddha P. Roy
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Chicken Breast ◽  
Thiol Groups ◽  
Dystrophic Muscle ◽  
Muscle Enzymes ◽  
Chicken Muscle ◽  
Dystrophic Chicken

The major14C-labelled peptides from creatine kinase from normal and dystrophic chicken muscle obtained by carboxymethylating the reactive thiol groups with iodo[2-14C]acetic acid and digestion with trypsin were purified by ion-exchange chromatography on Dowex-50 (X2) and by paper electrophoresis. The chromatographic characteristics of the14C-labelled peptides, their electrophoretic mobilities at pH6.5, and their amino acid compositions were identical for the two enzymes. The sequence of amino acids around the essential thiol groups of creatine kinase from normal and dystrophic chicken muscle was shown to be Ile-Leu-Thr-CmCys-Pro-Ser-Asn-Leu-Gly-Thr-Gly-Leu-Arg (CmCys, carboxymethylcysteine). This sequence is almost identical with that for the creatine kinases in human and ox muscle and bovine brain and is very similar to that of arginine kinase from lobster muscle. Antibodies to the enzymes were raised in rabbits and their reaction with the creatine kinase from normal and dystrophic muscles in interfacial, immunodiffusion and immunoelectrophoretic experiments was studied. The cross-reaction between normal muscle creatine kinase and antisera against the dystrophic muscle enzyme (or vice versa) observed by immunodiffusion and by immunoelectrophoretic experiments further suggests that the enzymes from normal and dystrophic chicken muscle are similar in structure. The results of the present study, the identical amino acid sequence of the peptides containing the reactive thiol group from both the normal and dystrophic chicken muscle enzymes and the immunological similarities of the two enzymes are in accord with the similarity of the two enzymes observed by Roy et al. (1970).

Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding protein

1990 ◽  
Vol 10 (8) ◽  
pp. 4116-4122
Author(s):  
Y Matsui ◽  
A Kikuchi ◽  
S Araki ◽  
Y Hata ◽  
J Kondo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Reaction ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Bovine Brain ◽  
Subunit Structure ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Ras P21

We recently purified to near homogeneity a novel type of regulatory protein for smg p25A, a ras p21-like GTP-binding protein, from bovine brain cytosol. This regulatory protein, named smg p25A GDP dissociation inhibitor (GDI), regulates the GDP-GTP exchange reaction of smg p25A by inhibiting dissociation of GDP from and subsequent binding of GTP to it. In the present studies, we isolated and sequenced the cDNA of smg p25A GDI from a bovine brain cDNA library by using an oligonucleotide probe designed from the partial amino acid sequence of purified smg p25A GDI. The cDNA has an open reading frame that encodes a protein of 447 amino acids with a calculated Mr of 50,565. This Mr is similar to those of the purified smg p25A GDI estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sucrose density gradient ultracentrifugation, which are about 54,000 and 65,000, respectively. The isolated cDNA is expressed in Escherichia coli, and the encoded protein exhibits GDI activity. smg p25A GDI is hydrophilic overall, except for one hydrophobic region near the N terminus. smg p25A GDI shares low amino acid sequence homology with the Saccharomyces cerevisiae CDC25-encoded protein, which has been suggested to serve as a factor that regulates the GDP-GTP exchange reaction of the yeast RAS2-encoded protein, but not with the beta gamma subunits of GTP-binding proteins having an alpha beta gamma subunit structure, such as Gs and Gi. The smg p25A GDI mRNA was present in various tissues, including not only tissues in which smg p25A was detectable but also tissues in which it was not detectable. This fact has raised the possibility that smg p25A GDI interacts with another G protein in tissues in which smg p25A is absent.

Amino-Acid Sequence of Human and Bovine Brain Myelin Proteolipid Protein (Lipophilin) is Completely Conserved

1985 ◽  
Vol 366 (2) ◽  
pp. 627-636 ◽  
Author(s):  
Wilhelm STOFFEL ◽  
Helmut GIERSIEFEN ◽  
Heinz HILLEN ◽  
Werner SCHROEDER ◽  
Budi TUNGGAL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolipid Protein ◽  
Bovine Brain ◽  
Myelin Proteolipid Protein ◽  
Myelin Proteolipid

scholarly journals Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein.

1991 ◽  
Vol 11 (5) ◽  
pp. 2873-2880 ◽  
Author(s):  
K Kaibuchi ◽  
T Mizuno ◽  
H Fujioka ◽  
T Yamamoto ◽  
K Kishi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Reaction ◽  
Binding Proteins ◽  
Bovine Brain ◽  
Rat Tissues ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Ras P21 ◽  
Exchange Protein

We have recently purified to near homogeneity the stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like GTP-binding proteins) from bovine brain cytosol. This regulatory protein, named GDP dissociation stimulator (GDS), stimulates the GDP/GTP exchange reaction of smg p21s by stimulating the dissociation of GDP from and the subsequent binding of GTP to them. In this study, we have isolated and sequenced the cDNA of smg p21 GDS from a bovine brain cDNA library by using an oligonucleotide probe designed from the partial amino acid sequence of the purified smg p21 GDS. The cDNA has an open reading frame encoding a protein of 558 amino acids with a calculated Mr value of 61,066, similar to the Mr of 53,000 estimated for the purified smg p21 GDS by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sucrose density gradient ultracentrifugation. The isolated cDNA is expressed in Escherichia coli, and the encoded protein exhibits smg p21 GDS activity. smg p21 GDS is overall hydrophilic, but there are several short hydrophobic regions. The smg p21 GDS mRNA is present in bovine brain and various rat tissues. smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi.

Amino-Acid Sequence Around the Reactive Thiol Groups of Adenosine Triphosphate–creatine Phosphotransferase

Nature ◽  
1964 ◽  
Vol 203 (4942) ◽  
pp. 267-269 ◽  
Author(s):  
A. R. THOMSON ◽  
J. W. EVELEIGH ◽  
B. J. MILES
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Adenosine Triphosphate ◽  
Thiol Groups

Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol

1987 ◽  
Vol 166 (2) ◽  
pp. 333-338 ◽  
Author(s):  
Francoise SCHOENTGEN ◽  
Florence SACCOCCIO ◽  
Jacqueline JOLLES ◽  
Ida BERNIER ◽  
Pierre JOLLES
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bovine Brain ◽  
Complete Amino Acid Sequence ◽  
Brain Cytosol
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