Identification of amino acid residues photolabeled with 2-azido[.alpha.-32P]adenosine diphosphate in the .beta. subunit of beef heart mitochondrial F1-ATPase

Biochemistry ◽  
1986 ◽  
Vol 25 (15) ◽  
pp. 4431-4437 ◽  
Author(s):  
Jerome Garin ◽  
Francois Boulay ◽  
Jean Paul Issartel ◽  
Joel Lunardi ◽  
Pierre V. Vignais
Keyword(s):  
Amino Acid ◽  
Adenosine Diphosphate ◽  
Beta Subunit ◽  
Beef Heart ◽  
Amino Acid Residues ◽  
F1 Atpase

Mutational replacements of conserved amino acid residues in the α subunit change the catalytic properties of Escherichia coli F1-ATPase

1989 ◽  
Vol 268 (2) ◽  
pp. 643-648 ◽  
Author(s):  
Satoshi Soga ◽  
Takato Noumi ◽  
Michiyasu Takeyama ◽  
Masatomo Maeda ◽  
Masamitsu Futai
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Catalytic Properties ◽  
Amino Acid Residues ◽  
Α Subunit ◽  
F1 Atpase

scholarly journals Recognition of the Beta-subunit of human chorionic gonadotropin and sub-determinants by target tissue receptors

1978 ◽  
Vol 176 (2) ◽  
pp. 599-602 ◽  
Author(s):  
S Ramakrishnan ◽  
C Das ◽  
G P Talwar
Keyword(s):  
Amino Acid ◽  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Leydig Cells ◽  
Beta Subunit ◽  
Peptide Sequence ◽  
Target Tissue ◽  
Amino Acid Residues ◽  
Testosterone Production ◽  
Tissue Receptors

The beta-subunit of human chorionic gonadotropin, purified immunochemically to eliminate undissociated human chorionic gonadotropin, induced testosterone production by mouse Leydig cells at concentrations 400-fold higher than human chorionic gonadotropin. Steroidogenesis was also stimulated by a synthetic fragment of the beta-subunit of human chorionic gonadotropin conforming to the peptide sequence residues 39–71, whereas peptide sequence residues 39–56 and three C-terminal fragments (residues 115–145, 111–145 and 101–145) failed to cause steroidogenesis. These studies suggest the presence in the beta-subunit of human chorionic gonadotropin of determinants recognized by the tissue receptors, a part of these determinants residing between amino acid residues 57–71.

scholarly journals Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II.

1987 ◽  
Vol 7 (10) ◽  
pp. 3409-3417 ◽  
Author(s):  
A Saxena ◽  
R Padmanabha ◽  
C V Glover
Keyword(s):  
Molecular Weight ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Protein Kinase ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Open Reading Frame ◽  
Beta Subunit ◽  
Amino Acid Residues ◽  
Reading Frame

Cloned cDNAs encoding both subunits of Drosophila melanogaster casein kinase II have been isolated by immunological screening of lambda gt11 expression libraries, and the complete amino acid sequence of both polypeptides has been deduced by DNA sequencing. The alpha cDNA contained an open reading frame of 336 amino acid residues, yielding a predicted molecular weight for the alpha polypeptide of 39,833. The alpha sequence contained the expected semi-invariant residues present in the catalytic domain of previously sequenced protein kinases, confirming that it is the catalytic subunit of the enzyme. Pairwise homology comparisons between the alpha sequence and the sequences of a variety of vertebrate protein kinase suggested that casein kinase II is a distantly related member of the protein kinase family. The beta subunit was derived from an open reading frame of 215 amino acid residues and was predicted to have a molecular weight of 24,700. The beta subunit exhibited no extensive homology to other proteins whose sequences are currently known.

scholarly journals Is pyrophosphate an analog of adenosine diphosphate for beef heart mitochondrial F1-ATPase.

1987 ◽  
Vol 262 (28) ◽  
pp. 13538-13544
Author(s):  
J P Issartel ◽  
O Favre-Bulle ◽  
J Lunardi ◽  
P V Vignais
Keyword(s):  
Adenosine Diphosphate ◽  
Beef Heart ◽  
F1 Atpase
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