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

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

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

The C-reactive proteins (CRP) from both rat and Limulus 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.     

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

Summary 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.     

Stress by restraining potentiates morphine catalepsy in rats

Summary Restraint-induced stress potentiated morphine catalepsy in rats. This potentiation was partially antagonized by pharmacologic treatments decreasing central serotonin, acetylcholine, prostaglandins and by naloxone. Selective increase in central dopamine also inhibited the potentiation.Acknowledgments. SKB is an ECFMG Senior Faculty Fellow from the Department of Pharmacology, Institute of Medical Sciences, Banaras Hindu University, Varanasi, India. Partial research support by the Dakota State Aerie Fraternal Order of Eagles is gratefully acknowledged.     

Restoration of photoreceptor ultrastructure and function in retinal degeneration slow mice by gene therapy

The gene Prph2 encodes a photoreceptor-specific membrane glycoprotein, peripherin-2 (also known as peripherin/rds), which is inserted into the rims of photoreceptor outer segment discs in a complex with rom-1 (ref. 2). The complex is necessary for the stabilization of the discs, which are renewed constantly throughout life, and which contain the visual pigments necessary for photon capture. Mutations in Prph2 have been shown to result in a variety of photoreceptor dystrophies, including autosomal dominant retinitis pigmentosa and macular dystrophy. A common feature of these diseases is the loss of photoreceptor function, also seen in the retinal degeneration slow (rds or Prph2 Rd2/Rd2) mouse, which is homozygous for a null mutation in Prph2. It is characterized by a complete failure to develop photoreceptor discs and outer segments, downregulation of rhodopsin and apoptotic loss of photoreceptor cells. The electroretinograms (ERGs) of Prph2Rd2/Rd2 mice have greatly diminished a-wave and b-wave amplitudes, which decline to virtually undetectable concentrations by two months. Subretinal injection of recombinant adeno-associated virus (AAV) encoding a Prph2 transgene results in stable generation of outer segment structures and formation of new stacks of discs containing both perpherin-2 and rhodopsin, which in many cases are morphologically similar to normal outer segments. Moreover, the re-establishment of the structural integrity of the photoreceptor layer also results in electrophysiological correction. These studies demonstrate for the first time that a complex ultrastructural cell defect can be corrected both morphologically and functionally by in vivo gene transfer.     

Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q

Human inherited cataract is both clinically diverse and genetically heterogeneous. Here we report the identification of the first mutations affecting the major intrinsic protein of the lens, MIP, encoded by the gene MIP on 12q14. MIP is a member of the aquaporin family of membrane-bound water channels. The mutations identified are predicted to disturb water flux across the lens cell membrane.