Aspects of the reproductive biology of two archer fishes <Emphasis Type="Italic">Toxotes chatareus</Emphasis>, (Hamilton 1822) and <Emphasis Type="Italic">Toxotes jaculatrix</Emphasis> (Pallas 1767)

Various aspects of the reproductive biology of two archer fishes Toxotes chatareus and Toxotes jaculatrix were studied to describe gonad development, spawning season, sex ratio, and fecundity. Spawning season was assessed using monthly changes in gonadosomatic index (GSI) and histological inspection of the gonads. Both species exhibit two modes of oocytes; a mode of small primary growth oocytes and a single mode that increases with size as oocytes sequester vitellogenin and undergo maturation, showing the synchronous oocyte development typical of total spawners. Based on GSI values and advanced stages of oocyte maturity, T. chatareus and T. jaculatrix, females appear to spawn from November to December. The average fecundity of female T. chatareus was 55 000 ± 5538 eggs, and T. jaculatrix was 50 000 ± 3440 eggs; fecundity ranged from 20 000 to 150 000 eggs for both species, with relative fecundities of 600 to 1100 eggs/g body weight, and a mean value of 800 ± 32 for T. chatareus; relative fecundity ranged from 500 to 1100 with a mean value of 700 ± 23 for T. jaculatrix. Sex ratio, defined as the proportion of males to females, was 2.2 and 2.5 in T. chatareus and T. jaculatrix, respectively. The apparent abundance of males in samples could be due to females being positioned lower in the water column and therefore being sampled less frequently. Our results indicate that in both species, spawning occurs between the months of November and December during the monsoon season, which provides the mangrove coastal waters inhabited by these species with an abundance of food resources and additional floodplain nursery habitat for larvae and juveniles.     

Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium.

When subjected to the stress of growth in a relatively low-salt environment (1.25 M NaCl), the halophilic bacterium Halobacterium halobium induces a catalase. The protein has been purified to electrophoretic homogeneity and has an M(r) of 240,000 and a subunit size of approximately 62,000. The enzyme is active over a broad pH range of 6.5 to 10.0, with a peak in activity at pH 7.0. It has an isoelectric point of 4.0. This catalse, which is not readily reduced by dithionite, shows a Soret peak at 406 nm. Cyanide and azide inhibit the enzyme at micromolar concentrations, whereas maleimide is without effect. The addition of 20 mM 3-amino-1,2,4-triazole results in a 33% inhibition in enzymatic activity. The tetrameric protein binds NADP in a 1:1 ratio but does not peroxidize NADPH, NADH, or ascorbate. Although the enzymatic activity is maximal when assayed in a 50 mM potassium phosphate buffer with no NaCl, prolonged incubation in a buffer lacking NaCl results in inactive enzyme. Moreover, purification must be performed in the presence of 2 M NaCl. Equally as effective in retaining enzymatic function are NaCl, LiCl, KCl, CsCl, and NH4Cl, whereas divalent salts such as MgCl2 and CaCl2 result in the immediate loss of activity. The catalase is stained by pararosaniline, which is indicative of a glycosidic linkage. The Km for H2O2 is 60 mM, with inhibition observed at concentrations in excess of 90 mM. Thus, the mesohalic catalase purified from H. halobium seems to be similar to other catalases, except for the salt requirements, but differs markedly from the constitutive halobacterial hydroperoxidase.