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Comparison of histidine decarboxylases from rat stomach and brain with that from whole bodies of rat fetus
- Source :
- Agents and actions. 14(2)
- Publication Year :
- 1984
-
Abstract
- Histidine decarboxylases from the stomach and brain of adult rats were purified 380- and 160-fold, respectively, and their properties compared with those of the enzyme from whole bodies of fetal rats (7600-fold purification). The molecular weights (about 90,000) and the apparent Km values for L-histidine (3 X 10(-4) M) of the three enzymes were similar. The pI value of the fetal enzyme was 5.0, and that of the brain enzyme was 5.4. Histidine decarboxylase of the stomach showed two peaks of activity corresponding to those of the fetal and brain enzymes (pI's of 5.0 and 5.4) on isoelectric focusing. Anti-fetal-histidine decarboxylase antiserum inhibited the stomach and fetal enzymes extensively, but the brain enzyme only slightly. These results indicate that there are at least two types of histidine decarboxylase in rat tissue.
- Subjects :
- Male
Carboxy-Lyases
Immunology
Antigen-Antibody Complex
Biology
Histidine Decarboxylase
Toxicology
Chromatography, DEAE-Cellulose
Fetus
Pregnancy
medicine
Animals
Pharmacology (medical)
Histidine
Pharmacology
chemistry.chemical_classification
Antiserum
Molecular mass
Isoelectric focusing
Stomach
Immune Sera
Brain
Rats, Inbred Strains
Histidine decarboxylase
Molecular biology
Rats
Kinetics
medicine.anatomical_structure
Enzyme
Biochemistry
chemistry
Chromatography, Gel
Female
Isoelectric Focusing
Subjects
Details
- ISSN :
- 00654299
- Volume :
- 14
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Agents and actions
- Accession number :
- edsair.doi.dedup.....e15f3dbf36f6b4565da0aeea0c102957