Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Trimeresurus”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 289 records · Page 16Linked to original sources
PubMed1993

Characterization of three fibrinogenolytic proteases isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus).

Snake venoms, particularly those belonging to Crotalidae and Viperidae families, are known to possess fibrinogenolytic proteases which strongly affect the blood coagulation system. Three fibrinogenolytic enzymes, named as TM-1, TM-2 and TM-3, were purified from the venom of Taiwan habu using anion-exchange and gel-filtration chromatographies followed by cation-exchange HPLC. These enzyme fractions were shown to be homogeneous as judged by SDS-gel electrophoresis. Further characterization of these purified fractions with fibrinogenase activity indicated that they are single-chain proteases possessing basic isoelectric points and molecular masses of approximately 27 kDa. These enzymes cleaved alpha-chain of fibrinogen first and then beta-chain, with relatively low activity on gamma-chain. Fibrinogenolytic activities of these enzymes were not significantly affected at extreme pH values, activity loss occurred only at temperatures higher than 65 degrees C. Enzyme activities were strongly inhibited by some metal chelators such as EDTA or 1,10-phenanthroline, suggesting that these fibrinogenases belong to metalloproteases. The closely similar amino-acid compositions coupled with identical cleaved products of similar molecular masses observed on the autolysis of TM-1 and TM-2 suggest that these two proteases are similar in primary structures and probably mutually related.

Amino Acids↗
PubMed1996

Primary structure of alboaggregin-B purified from the venom of Trimeresurus albolabris.

The complete amino acid sequences of alpha and beta subunits of alboaggregin-beta are presented. The alpha and beta subunits were separated by reversed-phase HPLC after reduction and S-pyridylethylation, and their sequences were determined by analysis of peptides generated by enzymatic or chemical digestion. The alpha and beta subunits consist of 133 and 123 amino acid residues, respectively. The sequences are highly homologous to each other (41.4% identity) and also to those of the alpha and beta subunits of botrocetin (a von Willebrand factor modulator) and the A and B chains of factor IX/X binding protein from other snake venoms. It is also homologous to C-type lectins with a homodimeric structure, but it shows no lectin-like activity.

Amino Acid Sequence↗
PubMed1996

Distribution of NADPH-diaphorase in the central nervous system of an infrared-sensitive snake, Trimeresurus flavoviridis.

The distribution of NADPH-diaphorase (NADPH-d) activity was studied in the central nervous system of an infrared sensitive snake. An inhibitor of nitric oxide synthase, dichloroindophenol (DPIP), was used to distinguish the characteristics of NADPH-d activity. Intensely and weakly NADPH-d-stained neurons and fibers were found in discrete regions throughout the snake brain and cervical spinal cord, such as the olfactory bulb, subcommissural organ, stratum griseum periventriculare, locus coeruleus, dorsal root, dorsal horn, and area X. It was particularly noticed that the trigeminal descending nuclei and reticular formation of the medulla oblongata contained many positive neurons and fibers, but the lateral descending nucleus and nucleus reticularis caloris (infrared sensory nuclei) certainly did not. The positive neurons and fibers were also observed in supraspinal sensory ganglia. DPIP inhibited NADPH-d activity in all regions except for the olfactory/vomeronasal nerve and glomeruli. The results prove for the first time the presence of NADPH-d activity in the ophidian brain and suggest that nitric oxide may be involved in many neural functions, but not in infrared sensory processing.

Animals↗