scholarly journals The Genes for Mouse Salivary Androgen-Binding Protein (ABP) Subunits Alpha and Gamma Are Located on Chromosome 7

Genetics ◽  
1987 ◽  
Vol 115 (3) ◽  
pp. 535-543
Author(s):  
Stephen R Dlouhy ◽  
Benjamin A Taylor ◽  
Robert C Karn

ABSTRACT We demonstrate that the previously described gene Androgen binding protein (Abp; Dlouhy and Karn, 1984) codes for the Alpha subunit of ABP and rename the locus Androgen binding protein alpha (Abpa). A study of recombinant inbred strains demonstrates that Abpa is located on chromosome 7 near Glucose phosphate isomerase-1 (Gpi-1). Biochemical and genetic evidence indicates the existence of another ABP subunit, Gamma, and its locus, Androgen binding protein gamma (Abpg), that is closely linked to Abpa. Although no polymorphism has yet been found for the previously described Beta subunit of ABP (Dlouhy and Karn, 1983; 1984), we suggest that it represents a third locus, Androgen binding protein beta (Abpb). ABP subunits appear to dimerize randomly and a model is presented demonstrating the origin of six ABP dimers in the salivas of AbpaaAbpga/AbpabAbpgb heterozygous mice. The results of cell-free translation studies in which the pre-ABP subunits are identified specifically by immunoprecipitation with anti-ABP antibody supports the idea that independent mRNAs code for the Alpha, Beta and Gamma subunits.

2004 ◽  
Vol 71 (5) ◽  
pp. 1461-1468 ◽  
Author(s):  
David M. Selva ◽  
Oscar M. Tirado ◽  
Nuria Toràn ◽  
Carlos A. Suárez-Quian ◽  
Jaume Reventos ◽  
...  

1997 ◽  
Vol 56 (1) ◽  
pp. 21-32 ◽  
Author(s):  
David R. Joseph ◽  
Deborah A. O’Brien ◽  
Patrick M. Sullivan ◽  
Marzia Becchis ◽  
James K Tsuruta ◽  
...  

2013 ◽  
Vol 76 (5) ◽  
pp. 324-331 ◽  
Author(s):  
Michael W. Vandewege ◽  
Carleton J. Phillips ◽  
Jeffrey K. Wickliffe ◽  
Federico G. Hoffmann

1987 ◽  
Vol 243 (1) ◽  
pp. 293-296 ◽  
Author(s):  
M E Baker ◽  
F S French ◽  
D R Joseph

Vitamin K-dependent protein S belongs to the family of clotting factors (e.g. Factors IX and X, and protein C). Unlike the other clotting factors, the C-terminal half (residues 250-634) of protein S is not a serine proteinase. In fact, the function of residues 250-634 of protein S is unknown. By using computer programs designed to detect evolutionary relationships between proteins, we find that this part of protein S is similar to rat androgen-binding protein, a protein produced and secreted by testicular Sertoli cells. The homology between protein S and androgen-binding protein suggests new approaches for elucidating their functions.


1974 ◽  
Vol 5 (4) ◽  
pp. 333-334
Author(s):  
E.J. Podesta ◽  
R.S. Calandra ◽  
M.A. Rivarola ◽  
J.A. Blaquier

Author(s):  
V. Hansson ◽  
S. C. Weddington ◽  
O. Naess ◽  
A. Attramadal ◽  
F. S. French ◽  
...  

Author(s):  
R. Guerrero ◽  
E. M. Ritzen ◽  
K. Purvis ◽  
V. Hansson ◽  
F. S. French

Author(s):  
Jacques I. Quivy ◽  
Raymond Devis ◽  
Xuan-Hoa Bui ◽  
Jean-Pierre Schmit ◽  
Guy G. Rousseau

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