Rat liver microsomal and lysosomal beta-glucuronidases differ in both carbohydrate and amino acid compositions.
AUTOR(ES)
Tulsiani, D R
RESUMO
To investigate the chemical relationships between rat liver lysosomal and microsomal beta-D-glucuronidases (EC 3.2.1.31), which are essentially identical catalytically and in reactivity with antibody and similar in molecular weight, the two enzymes were isolated by procedures in which modifications of the proteins were avoided. The purified enzymes were found to differ in both sugar and amino acid compositions. The microsomal enzyme contained much more mannose and, in contrast to the lysosomal enzyme, contained sialic acid but no glucose. Moreover, although the amino acid compositions generally agreed closely, the microsomal enzyme contained much more serine and somewhat less arginine than the lysosomal form. These findings of specific differences in composition should have a bearing on the consideration of intracellular glycoprotein synthesis, translocation, and compartmentalization.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=392717Documentos Relacionados
- Overlapping evolutionary affinities revealed by comparison of amino acid compositions.
- Nucleotide and deduced amino acid sequence of human liver microsomal epoxide hydrolase.
- Nucleotide and deduced amino acid sequence of rat liver 17 beta-hydroxysteroid UDP-glucuronosyltransferase.
- Structure of HLA antigens: amino-acid and carbohydrate compositions and NH2-terminal sequences of four antigen preparations.
- Purified membrane and soluble folate binding proteins from cultured KB cells have similar amino acid compositions and molecular weights but differ in fatty acid acylation.
