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Multiple forms of arylalkylamine N-acetyltransferase (NAT) from cockroach female colleterial glands and activity changes during oocyte maturation
- Source :
- Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 134:795-803
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- Arylalkylamine N-acetyltransferase (NAT) from the female colleterial glands of Periplaneta americana showed activity peaks at pH 6.0 and 9.5 and the pH profile changed during oogenesis. The left gland contained higher activity than the right gland but the right gland also contained recognizable activity. The patterns in activity change depended on the substrate used, tryptamine (TN) or serotonin (5-HT). When TN was used as the substrate, the alkaline peak was higher than the acidic peak. In contrast, when 5-HT was used, the acidic peak was much higher than the alkaline peak. This suggests that at least two NATs are present in this species that are specific to pH and substrate species. Of the four combinations of the two pH ranges and two substrate indolamines, the enzyme activity that showed a similar change to the oocyte maturation was obtained in the combination of pH 6.0 and TN. TN was actually detected in the colleterial glands by fluorescent measurements according to Hess and Uderfriend [J. Pharmacol. Exp., 127 (1959) 175-177]. It peaked on the 6th day of emergence, which corresponded to the first rise of oocyte length and yolk accumulation, whereas a small peak appeared in the phase of the second rise. TN, or more likely N-acetyl TN, may therefore be involved in the regulation of oocyte maturation which could be a novel mechanism in oocyte maturation.
- Subjects :
- Tryptamine
food.ingredient
Arylamine N-Acetyltransferase
Physiology
Cockroaches
Biology
Biochemistry
Oogenesis
chemistry.chemical_compound
food
Yolk
Electrochemistry
medicine
Animals
Molecular Biology
Chromatography, High Pressure Liquid
Substrate (chemistry)
Hydrogen-Ion Concentration
Oocyte
Enzyme assay
medicine.anatomical_structure
chemistry
Indolamines
Oocytes
Arylalkylamine
biology.protein
Female
Subjects
Details
- ISSN :
- 10956433
- Volume :
- 134
- Database :
- OpenAIRE
- Journal :
- Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
- Accession number :
- edsair.doi.dedup.....85762f2ba3eeffbe8fa1d02ff499f092
- Full Text :
- https://doi.org/10.1016/s1095-6433(03)00013-8