Concanavalin A-Binding Enzymes of Crotalus scutulatus scutulatus Venom

Crotalus scutulatus scutulatus crude venom was separated into two fractions by Concanavalin A Sepharose 4B affinity chromatography. The proteins binding to Con A exhibited phosphomonoesterase (orthophosphoric monoester phosphohydrolase EC 3.1.3.2), phosphodiesterase, 5\u27-nucleotidase (5\u27-ribonucleotide phosphohydrolase EC 3.1.3.5), phospholipase A(phosphatidate 2-acylhydrolase EC 3.1.1 .4), hyaluronidase (hyaluronate glycanohydrolase EC 3.2.1 d), N-benzoyl-L-arginine ethyl esterase, p-toluenesulfonyl-L-arginine methyl esterase, L-amino acid oxidase (L-amino acid: 02 oxidoreductase [deaminating] EC 1.4.3.2), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5\u27-ribonucleotide phosphohydrolase EC 3.1.3.5) activities were not observed. The crude venom and the fraction containing the glycoproteins which bound to Con A were fractionated by DEAE Sephadex A-50 ion exchange chromatography. Each of these samples yielded fractions having caseinolytic activities

Concanavalin A-Nonbinding Enzymes of Crotalus scutulatus scutulatus Venom

Crotalus scutulatus scutulatus crude venom was separated into two fractions by Concanavalin A Sepharose 4B affinity chromatography. The Concanavalin A-nonbinding fraction (F-l) exhibited phosphomonoesterase (orthophosphoric monoester phosphohydrolase EC 3.1 .3.2), phosphodiesterase, 5 \u27-nucleotidase (5 \u27-ribonucleotide phosphohydrolase EC 3.1.3.5), phospholipase A (phosphatidate 2-acylhydrolase EC 3.1.1.4), hyaluronidase (hyaluronate glycanohydrolase EC 3.2.1.d), N-benzoyl-Larginine ethyl esterase, p-toluenesulfonyl-L-arginine methyl esterase, L-amino acid oxidase (L-amino acid: O2 oxidoreductase [deaminating] EC 1.4.3.2), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5 \u27-ribonudeotide phosphohydrolase EC 3.1.3.5) activities were not observed. DEAE Sephadex A-50 ion exchange chromatography by two stage elution of F-l yielded several fractions having proteinase activities. Proteinase activity was observed in the latter fractions of the first elution and in the fractions of the second elution

Gas Chromortographic Analyses of Biocrude-Producing Trees

Gas chromotographic procedures were used to compare commercial diesel fuel with cyclohexane, ether, and methanol extracts from various tree species. Standard n-paraffin hydrocarbons ranging from C-10 thru C-34 were used as standards. These analyses indicated that several extracts, notably those from Juniper virginiana (juniper) and Pinus echinata (pine) trees of Northeast Arkansas and the Brazilian tree Copaifera langsdorffii (copaiba), contain numerous hydrocarbon and selected chemical products which serve as potential renewable biocrude sources

The Clinical Rationale for the Sentry Bioconvertible Inferior Vena Cava Filter for the Prevention of Pulmonary Embolism

The Sentry inferior vena cava (IVC) filter is designed to provide temporary protection against pulmonary embolism (PE) during transient high-risk periods and then to bioconvert after 60 days after implantation. At the time of bioconversion, the device's nitinol arms retract from the filtering position into the caval wall. Subsequently, the stable stent-like nitinol frame is endothelialized. The Sentry bioconvertible IVC filter has been evaluated in a multicenter investigational-device-exemption pivotal trial (NCT01975090) of 129 patients with documented deep vein thrombosis (DVT) or PE, or at temporary risk of developing DVT or PE, and with contraindications to anticoagulation. Successful filter conversion was observed in 95.7% of patients at 6 months (110/115) and 96.4% at 12 months (106/110). Through 12 months, there were no cases of symptomatic PE. The rationale for development of the Sentry bioconvertible device includes the following considerations: (1) the period of highest risk of PE for the vast majority of patients occurs within the first 60 days after an index event, with most of the PEs occurring in the first 30 days; (2) the design of retrievable IVC filters to support their removal after a transitory high-PE-risk period has, in practice, been associated with insecure filter dynamics and time-dependent complications including tilting, fracture, embolization, migration, and IVC perforation; (3) most retrievable IVC filters are placed for temporary protection, but for a variety of reasons they are not removed in any more than half of implanted patients, and when removal is attempted, the procedure is not always successful even with advanced techniques; and (4) analysis of Medicare hospital data suggests that payment for the retrieval procedure does not routinely compensate for expense. The Sentry device is not intended for removal after bioconversion. In initial clinical use, complications have been limited. Long-term results for the Sentry bioconvertible IVC filter are anticipated soon

Enzymes in Heloderma horridum Venom

A mixture of venom and saliva from the lizard Heloderma horridum was analyzed for esterase, phosphomonoesterase, phosphodiesterase, 5\u27nucleotidase, and protease activities. Hydrolysis of N-benzoyl-L-arginine ethyl ester occurred at a pH optimum between pH 8.6 and 9.1 with a maximum activity of 452 units per mg per min. Hydrolysis of ptoluenesulfonyl-L-arginine methyl ester occurred at a pH optimum between pH 8.1 and 8.5 with a maximum of only 36 units per mg per min. One mg of the venom mixture liberated 9.3 μM of p nitrophenol from p-nitrophenyl phosphate per minute at an optimum pH between 8.2 and 8.3. Over a wide range of pH, only low phosphodiesterase and 5\u27nucleotidase activities were observed. A trace of caesinolytic activity occurred at pH 9.0

5\u27-Nucleotidase and Thrombin-Like Activities of Selected Crotalid Venoms

Thrombin-like activities were not observed inCrotalus basiliscus, C. molossus and C. scutulatus scutulatus crude venoms. 5\u27-Nucleotidase specific activities of 0.863, 0.273 and 5.520 units/mg of crude venom protein were observed inC. basiliscus, C. molossus and C. s. scutulatus venoms, respectively. Concanavalin ASepharose 4 B (Con A)affinitychromatography yielded two fractions from each of the crude venoms. Ineach instance, both fractions exhibited 5\u27-nucleotidase activities and the Con A-binding proteins had higher activities than the Con A-nonbinding proteins. 5\u27-Nucleotidase activities inthe DEAESephadex A-50 chromatographic fractions were localized in the first elution fraction and the last fraction(s) to elute. EDTAhad no effect on the 5\u27-nucleotidase activities ofthe crude venoms