Modulation of Diverse Procoagulant Venom Activities by Combinations of Platinoid Compounds

Procoagulant snake venoms have been inhibited by the ruthenium containing compounds CORM-2 and RuCl3 separately, presumably by interacting with critical histidine or other sulfur-containing amino acids on key venom enzymes. However, combinations of these and other platinoid containing compounds could potentially increase, decrease or not affect the procoagulant enzyme function of venom. Thus, the purpose of this investigation was to determine if formulations of platinoid compounds could inhibit venom procoagulant activity and if the formulated compounds interacted to enhance inhibition. Using a human plasma coagulation kinetic model to assess venom activity, six diverse venoms were exposed to various combinations and concentrations of CORM-2, CORM-3, RuCl3 and carboplatin (a platinum containing compound), with changes in venom activity determined with thrombelastography. The combinations of CORM-2 or CORM-3 with RuCl3 were found to enhance inhibition significantly, but not in all venoms nor to the same extent. In sharp contrast, carboplatin-antagonized CORM-2 mediated the inhibition of venom activity. These preliminary results support the concept that platinoid compounds may inhibit venom enzymatic activity at the same or different molecular sites and may antagonize inhibition at the same or different sites. Further investigation is warranted to determine if platinoid formulations may serve as potential antivenoms.

Download Full-text

Determining sulfur-containing amino acids by capillary electrophoresis: A fast novel method for total homocyst(e)ine human plasma

Electrophoresis ◽

10.1002/(sici)1522-2683(19990301)20:3<569::aid-elps569>3.0.co;2-s ◽

1999 ◽

Vol 20 (3) ◽

pp. 569-574 ◽

Cited By ~ 31

Author(s):

Gennaro Vecchione ◽

Maurizio Margaglione ◽

Elvira Grandone ◽

Donatella Colaizzo ◽

Giuseppe Cappucci ◽

...

Keyword(s):

Amino Acids ◽

Capillary Electrophoresis ◽

Human Plasma ◽

Novel Method ◽

Sulfur Containing

Download Full-text

Effects of Heme Modulation on Ovophis and Trimeresurus Venom Activity in Human Plasma

Toxins ◽

10.3390/toxins10080322 ◽

2018 ◽

Vol 10 (8) ◽

pp. 322 ◽

Cited By ~ 5

Author(s):

Vance G. Nielsen ◽

Nathaniel Frank ◽

Ryan W. Matika

Keyword(s):

Carbon Monoxide ◽

Enzymatic Activity ◽

Human Plasma ◽

The Other ◽

Geographic Isolation ◽

Diverse Species ◽

Fibrinogenolytic Activity ◽

Coagulation Kinetics ◽

Kinetics Of ◽

Coagulation Kinetic

Geographic isolation and other factors result in evolution-driven diversity of the enzymatic composition of venom of pit vipers in the same genus. The present investigation sought to characterize venoms obtained from such genetically diverse Ovophis and Trimeresurus pit vipers utilizing thrombelastographic coagulation kinetic analyses. The coagulation kinetics of human plasma were assessed after exposure to venom obtained from two Ovophis and three Trimeresurus species. The potency of each venom was defined (µg/mL required to equivalently change coagulation); additionally, venoms were exposed to carbon monoxide (CO) or a metheme-inducing agent to modulate any enzyme-associated heme. All venoms had fibrinogenolytic activity, with four being CO-inhibitable. While Ovophis venoms had similar potency, one demonstrated the presence of a thrombin-like activity, whereas the other demonstrated a thrombin-generating activity. There was a 10-fold difference in potency and 10-fold different vulnerability to CO inhibition between the Trimeresurus species. Metheme formation enhanced fibrinogenolytic-like activity in both Ovophis species venoms, whereas the three Trimeresurus species venoms had fibrinogenolytic-like activity enhanced, inhibited, or not changed. This novel “venom kinetomic” approach has potential to identify clinically relevant enzymatic activity and assess efficacy of antivenoms between genetically and geographically diverse species.

Download Full-text

Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

1982 ◽

Vol 40 ◽

pp. 294-295

Author(s):

E.M. Kuhn ◽

K.D. Marenus ◽

M. Beer

Keyword(s):

Amino Acids ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Electron Microscopic ◽

Good Correspondence ◽

Specific Staining ◽

Type Iii ◽

Different Types ◽

Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Download Full-text

Antioxidative status as assessed by enzymatic activity in the tear fluid and by the levels of sulfur-containing protein groups in the blood and tear fluid of myopes before and after treatment with a thiol agent

Oftalmologicheskii Zhurnal ◽

10.31288/oftalmolzh201743139 ◽

2017 ◽

Vol 68 (4) ◽

pp. 31-39 ◽

Cited By ~ 1

Author(s):

E. Surova ◽

◽

I. Boichuk ◽

S. Kolomiichuk ◽

◽

...

Keyword(s):

Enzymatic Activity ◽

Tear Fluid ◽

Antioxidative Status ◽

Before And After ◽

Sulfur Containing

Download Full-text

Model studies regarding the internal corrosion of tin-plated food cans. III. Binding of tin(II) ions and iron(II) ions by sulfur-containing amino acids

Journal of Agricultural and Food Chemistry ◽

10.1021/jf60186a015 ◽

1973 ◽

Vol 21 (2) ◽

pp. 246-251 ◽

Cited By ~ 4

Author(s):

Dieter W. Gruenwedel ◽

Hsien-Chung Hao

Keyword(s):

Amino Acids ◽

Internal Corrosion ◽

Model Studies ◽

Sulfur Containing

Download Full-text

Determination of Branched-Chain Amino Acids in Food Supplements and Human Plasma by a CE-MS/MS Method with Enhanced Resolution

International Journal of Molecular Sciences ◽

10.3390/ijms22158261 ◽

2021 ◽

Vol 22 (15) ◽

pp. 8261

Author(s):

Juraj Piestansky ◽

Michaela Matuskova ◽

Ivana Cizmarova ◽

Dominika Olesova ◽

Peter Mikus

Keyword(s):

Amino Acids ◽

Human Plasma ◽

Limit Of Detection ◽

Background Electrolyte ◽

Branched Chain Amino Acids ◽

Fused Silica ◽

Suitable Alternative ◽

Enhanced Resolution ◽

Validation Parameters ◽

Branched Chain

In the presented study, a capillary electrophoresis-mass spectrometry method combining high separation efficiency and sensitive detection has been developed and validated, for the first time, to quantify branched chain amino acids (valine, isoleucine, leucine) in commercial food and sport supplement samples and human plasma samples. The separations were performed in a bare fused silica capillary. The background electrolyte was composed of 500 mM formic acid with pH 2.0. The plasma sample pretreatment was realized by simple protein precipitation with acetonitrile. Injection of a short zone of highly basic electrolyte before the sample injection and application of the negative pressure on the separation were accompanied by enhanced resolution of the isobaric amino acids—isoleucine and leucine. The developed method was characterized by favorable validation parameters, such as linearity (r2 > 0.99), accuracy and precision, the limit of detection, lower limit of quantification, or robustness. These parameters were more than sufficient for the quantification of branched chain amino acids in various samples. The determined concentrations of branched chain amino acids in food and sports supplements were in very good agreement with the content declared by the manufacturer. The investigated concentrations of branched chain amino acids were in the range 294.68–359.24 µM for valine, 91.76–95.67 µM for isoleucine, and 196.78–251.24 µM for leucine. These concentrations fall within the physiological limits. The developed CE-MS/MS method represents a suitable alternative to traditional approaches used in branched chain amino acid quality control and bioanalysis.

Download Full-text

THE LIPOTROPIC ACTION OF SOME SULFUR-CONTAINING AMINO ACIDS AND RELATED SUBSTANCES

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)72885-8 ◽

1941 ◽

Vol 140 (1) ◽

pp. 27-34

Author(s):

Sam A. Singal ◽

H.C. Eckstein

Keyword(s):

Amino Acids ◽

Related Substances ◽

Sulfur Containing

Download Full-text

UTILIZATION OF SULFUR-CONTAINING AMINO ACIDS BY MUTANT STRAINS OF ESCHERICHIA COLI

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)57352-x ◽

1948 ◽

Vol 174 (2) ◽

pp. 717-722

Author(s):

Sofia. Simmonds

Keyword(s):

Escherichia Coli ◽

Amino Acids ◽

Mutant Strains ◽

Sulfur Containing

Download Full-text

Antibody to antihemophilic factor and its lack of reaction with hemophilic plasma

American Journal of Physiology-Legacy Content ◽

10.1152/ajplegacy.1965.208.3.499 ◽

1965 ◽

Vol 208 (3) ◽

pp. 499-507 ◽

Cited By ~ 6

Author(s):

William D. McLester ◽

Robert H. Wagner

Keyword(s):

Amino Acids ◽

Human Plasma ◽

Measurable Effect ◽

Rabbit Plasma ◽

Canine Plasma ◽

Inhibitor Titer ◽

Antihemophilic Factor ◽

Immune Rabbit

A partially purified preparation of canine antihemophilic factor was obtained utilizing amino acids as precipitating agents. This AHF preparation was used as the antigen in an immunologic investigation of canine hemophilia. Plasma from rabbits immunized with this preparation contained antibodies which inhibited the coagulation of normal canine plasma. The immune rabbit plasma inhibited AHF activity but had no measurable effect on any other procoagulant. Neither canine hemophilic plasma nor fractions prepared from canine hemophilic plasma contained an antigen capable of neutralizing the inhibitor (no cross-reacting material). The inhibitor titer was inversely proportional to the amount of added AHF in the form of a fraction of normal canine plasma. The inhibitor cross-reacted with human plasma AHF, but not with porcine, bovine, or rabbit AHF. The results of these studies are interpreted as providing further evidence that hemophilia, specifically canine hemophilia, is due to the failure of production of the antihemophilic factor.

Download Full-text