Partial amino acid sequence of sheep liver serine hydroxymethyltransferase and comparison of peptide maps of the enzyme from human, ox livers and Escherichia coli.
Indian J Biochem Biophys
;
1992 Apr; 29(2): 183-8
Article
in English
| IMSEAR
| ID: sea-26247
ABSTRACT
A comparison of the tryptic peptide maps of serine hydroxymethyltransferase from sheep, human, ox livers and Escherichia coli revealed that the mammalian enzymes were similar, while the bacterial enzyme exhibited differences in the primary structure. N-terminus of the reduced carboxymethylated sheep liver enzyme was acetylated. Serine hydroxymethyltransferase was hydrolyzed with trypsin and fragments of peptides were separated by high performance liquid chromatography using a combination of gel permeation, reverse phase and ion-pair chromatography. The peptides were sequenced manually using the 4-N,N'-dimethyl aminoazobenzene-4'-isothiocyanate/phenyl isothiocyanate double coupling method. The tryptic peptides with 80% homology or above were aligned on the rabbit liver enzyme sequence.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Peptide Fragments
/
Rabbits
/
Glycine Hydroxymethyltransferase
/
Peptide Mapping
/
Humans
/
Cattle
/
Sheep
/
Molecular Sequence Data
/
Amino Acid Sequence
/
Sequence Homology
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1992
Type:
Article
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