Abstract

Dynamics of tyrosine hydroxylase (TH) was studied in various brain regions and pituitary in relation to annual/seasonal and circadian variations in either sex of the catfish Heteropneustes fossilis. α-Methylparatyrosine inhibited TH activity significantly in a time—(in vivo study) and concentration—(in vitro study) dependent manner. The inhibition was higher in resting phase than preparatory phase and in females than males (time-course study). The apparent kinetic constant of inhibition ( K i) varied both seasonally and regionally. The values were higher in resting phase and in the forebrain regions (telencephalon and hypothalamus) than medulla oblongata. No significant sex difference was noticed in the K i values in the same season. TH activity showed significant annual/seasonal variations with telencephalon and hypothalamus showing higher activity than medulla oblongata. The females showed significantly higher enzyme activity than males with a distinct activity peak in June (prespawning phase). Such an activity peak was apparently absent in males. TH activity showed significant circadian/diurnal variations, the highest activity was noticed at 12 h and the lowest at 24 h. The apparent Michaelis–Menten constant ( K m) values (hypothalamic TH) for substrate ( l-tyrosine) and cofactor (DMPH 4) showed seasonal variations with the highest values in the resting phase, decreasing through preparatory and prespawning phases, to the lowest values in spawning phase. V max was the lowest in the resting phase and highest in the spawning phase. TH activity was low in the pituitary and could be detected in pooled samples from March (preparatory phase) to July (spawning phase). Activity showed significant variations, which could be correlated with the gonadosomatic index. The results show that TH activity could be positively correlated with the annual reproductive cycle. The enzyme activity could be also correlated with seasonal, sex, and regional variations in the apparent K m and V max values suggesting apparent differences in the affinity of the enzyme towards substrate and cofactor.

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