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Literature summary for 2.4.1.38 extracted from

  • Boeggeman, E.E.; Ramakrishnan, B.; Qasba, P.K.
    The N-terminal stem region of bovine and human beta1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies (2003), Protein Expr. Purif., 30, 219-229.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
stem region fused to the catalytic domain, expression in Escherichia coli Homo sapiens
stem region fused to the catalytic domain, expression in Escherichia coli Bos taurus

General Stability

General Stability Organism
the N-terminal stem extension enhances the in vitro folding efficiency of the catalytic domain by several fold, it increases the solubility of even the misfolded protein Homo sapiens
the N-terminal stem extension enhances the in vitro folding efficiency of the catalytic domain by several fold, it increases the solubility of even the misfolded protein Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
the folding efficiency of the catalytic domain is increased further if the protein is renatured in a buffer that has polyethylene glycol and L-arginine Homo sapiens
the folding efficiency of the catalytic domain is increased further if the protein is renatured in a buffer that has polyethylene glycol and L-arginine Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
placenta
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
beta1,4-galactosyltransferase I
-
Homo sapiens
beta1,4-galactosyltransferase I
-
Bos taurus