Immunological identity of the two different molecular mass constitutive subunits of liver arginase.
A detailed understanding of the regulatory mechanisms of arginase in the cell will depend on the clarification of the origin of the two different molecular mass subunits and on the arrangements of them to constitute the native enzyme. Here, we show the immunological recognition of the 39.5 and 37.0 kDa subunits of arginase by antibodies against both subunits. We also find that the subunit stoichiometry (39.5 kDa: 37.0 kDa) present in purified arginase preparations as well as in fresh isolated microsomes and cytoplasm corresponds to 3:1, indicating high prevalence of a constant arrangement of the constitutive subunits of arginase. These findings represent evidence for a limited posttranscriptional or posttranslational modification of only a fraction of the synthesized arginase in liver.
Diez
A
A
Departamento de Bioquímica y Biología Molecular y Genética, Universidad de Extremadura, Facultad de Veterinaria, Cáceres, Spain.
Fuentes
J M
JM
Prada
F
F
Campo
M L
ML
Soler
G
G
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D001119:Arginase / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D015153:Blotting, Western; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D008970:Molecular Weight; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar
D000911:Antibodies, Monoclonal; D001119:Arginase