Search PubMed⌕ Search

Biomedical subjects

R S Criddle

Publications and source records attributed to R S Criddle.

At least 37 records · Page 2Linked to original sources
PubMed1987

Protein composition of the threat induced epidermal secretion from the Arabian Gulf catfish, Arius thalassinus (Ruppell).

1. When threatened or injured, the Arabian Gulf catfish (Arius thalassinus, Ruppell) secretes a thick gel-like layer of proteinaceous material to its skin surface mainly from unicellular glands of the epidermis termed club cells. 2. Since a preparation from this secretion has been implicated in stimulation of the rate of wound healing in man and other test animals, the total gel protein composition was analysed by chemical, chromatographic and electrophoretic techniques. 3. Gel proteins were separated into soluble and insoluble fractions by extractions with increasingly strong solubilizing agents and the most insoluble components were solubilized only upon treatment with 10% SDS or concentrated organic acids. 4. Some of the soluble proteins from the secretion are also present in the insoluble protein fractions, indicating that the insoluble material is formed in part by aggregation of the soluble proteins. 5. The secretion was shown to be distinct from the catfish venom and differed greatly from typical fish mucus secretions in its composition and distribution of protein components.

Amino Acids↗
PubMed1986

Vasoconstrictor components in the Arabian Gulf catfish (Arius thalassinus, Ruppell) proteinaceous skin secretion.

The Arabian Gulf catfish (Arius thalassinus, Ruppell) produces toxic substances from its skin and from venom glands located near the base of the pectoral fins. Investigation of the pharmacological properties of the skin toxin have previously shown cholinergic vasoconstrictor activity in umbilical arteries. Cholinergic vasoconstriction was confirmed in sheep renal arteries. This activity was partially blocked by atropine, while most of the residual contraction was eliminated by simultaneous addition of indomethacin. Skin toxin treatment of arterial specimens caused a release of prostaglandin (PGE2, TXB2 and 6-keto-PGF1 alpha) into the organ bath. Prostaglandin release was blocked by pretreatment with indomethacin. Heat denaturation of skin toxin caused a loss of only the indomethacin-sensitive muscle contraction activity; most of the residual activity was blocked by atropine.

Animals↗
PubMed1986

Purification and properties of a hemagglutination factor from Arabian Gulf catfish (Arius thalassinus) epidermal secretion.

A galactose specific lectin was isolated from an epidermal proteinaceous gel secretion of the Arabian Gulf catfish, Arius thalassinus, Ruppell. The lectin was extracted and purified to near homogeneity by exclusion chromatography, affinity chromatography and isoelectric focusing. The lectin appears to be active as a single polypeptide chain with a mol. wt near 200,000, which can form oligomers and heteropolymers. The lectin comprises about 2% of the total gel protein, lacks carbohydrates and contains no unusual types or amounts of amino acids. The lectin agglutinates a wide range of red blood cell types.

Animals↗
PubMed1986

Lipid composition of the epidermal gel secretion from the Arabian Gulf catfish (Arius thalassinus Ruppell).

Lipids associated with a threat induced epidermal gel secretion from the catfish, Arius thalassinus, have been analyzed. Phospholipids, neutral lipids and glycolipids are all present and each of these subclasses has been analyzed by thin layer and gas chromatography with a general similarity with membrane lipids being noted. The epidermal gel lipids differed from total liver lipids of the catfish. Fatty acid analysis showed the gel lipid to be rich in the unsaturated fatty acids: oleate (omega 7, C18:1), arachidonate (omega 6, C20:4), and docosahexaenoate (omega 3, C22:6). Some prostaglandins were quantitated in lipid extracts from the epidermal gel.

Animals↗
PubMed1985

Isolation and characterization of metmyoglobin reductase from yellowfin tuna (Thunnus albacares).

The isolation, purification, and characterization of metmyoglobin reductase from yellowfin tuna (Thunnus albacares) is described. The enzyme has been purified 120-fold. Characterization of the enzyme includes molecular weight, isoelectric point, substrate specificity, enzyme kinetics, chromatographic behavior, and sensitivity to inhibitors. The physical and catalytic properties of the tuna enzyme are compared to those of bovine and blue-white dolphin metmyoglobin reductase.

Animals↗
PubMed1983

An acyl-thioesterase from yeast mitochondria.

A previously unstudied acyl-coenzyme A thioesterase activity has been demonstrated in submitochondrial particles from Saccharomyces cerevisiae. The preferred substrate for the enzyme activity is oleoyl-coenzyme A. Tests with inhibitors of the thioesterase showed that, in addition to common thiol inhibitors, the oxidative phosphorylation inhibitors oligomycin and venturicidin also blocked thioesterase activity. Purification of the enzyme catalyzing this activity revealed that thioesterase copurified with mitochondrial ATPase. When thioesterase was isolated from oxidative phosphorylation mutants selected for resistance to these two inhibitors, thioesterase activity was also resistant. The results suggest that thioester hydrolysis may be catalyzed by components associated with the isolated ATPase complex. Further attempts to link this activity to in vivo function of ATPase were not successful.

Ethylmaleimide↗
PubMed1983

Vascular responses elicited by venom of Arabian catfish (Arius thallasinus).

The Arabian catfish produces venoms from the skin (SV) and glands near the pectoral spines (GV). 1. The venoms have a high protein concentration, only limited amounts of lipid, carbohydrate and nucleic acid. Enzyme activities included alkaline phosphatase and esterases. Both SV and GV induce hemolysis. 2. SV and GV induced a dose-dependent smooth muscle contraction of human umbilical artery preparations. This response was competitively inhibited by atropine, suggesting a cholinergic response. 3. Heat treatment of GV did not decrease activity, while heating SV reduced it. 4. In-vivo experiments showed mainly a depressor response in rat and guinea-pig.

Animals↗
PubMed1977

Oligomycin-dependent ionophoric protein subunit of mitochondrial adenosinetriphosphatase.

A proteolipid isolated from yeast mitochondrial adenosinetriphosphatase (subunit 9) (ATP phosphohydrolase; EC 3.6.1.3) by chloroform/methanol extraction has been shown to discharge photo-induced potentials across a planar phospholipid membrane containing bacteriorhodopsin. Oligomycin, a specific inhibitor of oxidative phosphorylation which binds to this protein, allows the potential gradient to be reestablished. When proteolipid was isolated from an oligomycin-resistant strain, ionophoric activity was still obtained but the effect was not reversed by oligomycin. These studies suggest that the hydrophobic subunit-9 polypeptide is the ionophoric component linking ATP synthesis (hydrolysis) with proton translocation.

Adenosine Triphosphatases↗
PubMed1977

F1-ATPase-catalyzed synthesis of ATP from oleoylphosphate and ADP.

Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 3.6.1.3) isolated from yeast mitochondria catalyze the reaction of oleoylphosphate with ADP to yield ATP and oleic acid. Formation of ATP is specifically inhibited by the F1-ATPase inhibitor 1799 and by dinitrophenol. In the presence of F1, dinitrophenol "uncouples" the synthase reaction by causing rapid hydrolysis of oleoylphosphate without ATP formation. It is proposed that this F1 catalyzed ATP synthesis reaction corresponds to the terminal chemical step in oxidative phosphorylation.

Adenosine Diphosphate↗