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Codfish muscle aldolase: Purification, properties, and primary structure around the substrate-binding site
- Source :
- Archives of Biochemistry and Biophysics. 144:467-475
- Publication Year :
- 1971
- Publisher :
- Elsevier BV, 1971.
-
Abstract
- FDP aldolase has been purified and crystallized from the muscle of codfish. The specific activity of the codfish enzyme was found to be two-thirds that of rabbit muscle aldolase. Other catalytic properties, the molecular weight, and the carboxyl-terminal structure were similar to those of rabbit muscle aldolase. A tryptic peptide containing the Schiff base-forming lysine (1) has been isolated and its primary structure determined as: Ala-Leu-Ser-Asp-His-His-Val-Tyr-Leu-Gln-Gly-Thr-Leu-Leu-βGlys-Pro-Asn-Met-Val-Thr-Ala-Gly-His-Ser-CMCys-Ser-His-Lys. Extensive homology observed in this region of the aldolase molecules isolated from biologically divergent sources indicates the importance of this structure for catalysis of the aldolase reaction.
- Subjects :
- Electrophoresis
Paper
Lysine
Biophysics
Carboxypeptidases
Methylation
Biochemistry
Catalysis
Acetone
Fructose-Bisphosphate Aldolase
Trioses
Animals
Chemical Precipitation
Chymotrypsin
Phosphoric Acids
Trypsin
Amino Acid Sequence
Amino Acids
Binding site
Molecular Biology
Schiff Bases
chemistry.chemical_classification
Carbon Isotopes
Binding Sites
Cyanides
biology
Sulfates
Aldolase B
Aldolase A
Fishes
Protein primary structure
Substrate (chemistry)
Hydrogen-Ion Concentration
Chromatography, Ion Exchange
Molecular Weight
Quaternary Ammonium Compounds
Enzyme
chemistry
Chromatography, Gel
biology.protein
Specific activity
Crystallization
Peptides
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 144
- Database :
- OpenAIRE
- Journal :
- Archives of Biochemistry and Biophysics
- Accession number :
- edsair.doi.dedup.....15a265d40bef312bdfbea43ee8a12084