Maturidade do ovário no cascudo Hypostomus strigaticeps (Siluriformes, Loriicaridae)

This work studied the ovarian development of the armored catfish Hypostomus strigaticeps. Between July 2002 and June 2005, 332 females were collected monthly from the Corumbatai River, São Paulo State [long dash] Brazil. The ovaries were processed using routine histological techniques [long dash] paraffin inclusion and 5 pm thick sections stained in hematoxylin-cosin. Six types of oocytes were observed: Chromatin-nucleolus, Perinncleolar, Cortical-alveolus, Vitellogenic, Ripe and Atresic. Four maturity stages were created based on macroscopic and microscopic morphological observations, as well as on analysis of the gonadossomatic index (GSI): Rest, Maturation, Ripe and Spawned.

Crystallization and preliminary X-ray diffraction analysis of a eumenine mastoparan toxin: a new class of mast-cell degranulating peptide in the wasp venom

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized and X-ray diffraction data collected to 2.7 Angstrom resolution using a synchrotron-radiation source. Crystals were determined to belong to the space group P6(2)22 (P6(4)22). This is the first mastoparan to be crystallized and will provide further insights into the conformational significance of mastoparan toxins with respect to their potency and activity in G-protein regulation.

Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 Angstrom resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 Angstrom. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation. (C) 3001 Elsevier B.V. B.V. All rights reserved.