Soumendu Bhattacharya

Binding property of rat andLimulus C-reactive proteins (CRP) to mercury

The C-reactive proteins (CRP) from both rat andLimulus were found to bind mercury (Hg) in both in vivo and in vitro conditions. CRP has high-affinity binding sites for Hg as evidenced by the loss of free sulfhydryl groups, arrested mobility in polyacrylamide gel electrophoresis, and the consumption of CRP in the serum after Hg administration. The binding was tight as it could not be inhibited either by the addition of cysteine or EDTA. By using a direct titration method it was shown that binding of Hg to CRP was saturable at a molar ratio of Hg/CRP=13.11. The possibility that CRP may act as a scavenger for Hg is discussed.

Interrelationship between plasma and ovarian cholesterol in a teleost fish

The profiles of plasma and ovarian cholesterol altered similarly as a result of seasonal influence. Fish pituitary extract and LH significantly depleted plasma and ovarian free cholesterol only, esterified cholesterol remaining unaltered. Findings indicated that plasma cholesterol was the primary source of sterol for ovarian steroidogenesis.

Bovine TSH-stimulation of fish thyroid peroxidase activity and role of thyroxine thereon.

bTSH augmented the fish thyroid peroxidase activity in a dose-response manner. Thyroxine could not modulate the effect of exogenous bTSH, but it decreased the peroxidase activity in a control system when administered alone. The data therefore suggest similar negative feedback control system for TSH-regulation as operative in the case of mammals.

In vitro demonstration of peroxidase activity in the fish kidney soluble supernatant and its physiological importance

In der Kopfniere des TeleostiersAnabes testudineus wurde eine besonders hohe Peroxidase-Aktivität nachgewiesen, insbesondere deren Iodid-Oxydation zu Tri-Iodid.

Thyroxine formation by fish kidney soluble supernatant ofAnabas testudineus

In der löslichen überstehenden Fraktion (105,000×g) der Kopfniere des KnochenfischesAnabas testudineus wurde ein Enzym nachgewiesen, welches die Synthese des Thyroxins katalysiert. Die Menge des löslichen Nierenproteins und die Inkubationszeit stellen zwei limitierende Faktoren für die in vitro-Synthese des Thyroxins dar.