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Biomedical subjects

R S Lane

Publications and source records attributed to R S Lane.

At least 109 records · Page 6Linked to original sources
PubMed1982

Response to infusions of polyelectrolyte fractionated human factor VIII concentrate in human haemophilia A and von Willebrand's disease.

Factor VIII was purified from cryoprecipitate by ion exchange chromatography on solid phase polyelectrolyte E-5 (PE-E5). The product was highly purified (3.5 u VIII:C/mg protein) compared to conventional concentrate (0.3 u VIII:C/mg protein) with low fibrinogen, low isoagglutinin titre, and a ratio of factor VIII coagulant activity (VIII:C) to factor VII related antigen (VIIIR:Ag) of 16:1. Trial infusions of this material (PE VIII) were given to three patients with severe haemophilia A and one patient with homozygous von Willebrand's disease. These patients also each received separate infusions of intermediate purity concentrate (IPC) for comparison. There were no adverse effects. The mean half life of VIII:C after PE VIII infusion in the haemophiliacs was 10.9 h and after IPC was 12.1 h, a statistically insignificant difference. The survival of factor VIII coagulant antigen (VIII:CAg) was similar to that of VIII:C. In contrast, the half life of VIII:C and of VIII:CAg was very short after infusion of PE VIII in the patient wih von Willebrand's disease (2.4 h). IPC when infused in this patient produced a typical secondary rise of VIII:C. Two bleeding episodes in severe haemophiliacs were satisfactorily treated with PE VIII. PE-E5 deserves further study as a means of preparing clinical concentrates of factor VIII.

Antigens↗
PubMed1982

Identification of an isolate of Rickettsia canada from California.

A strain of Rickettsia canada was recovered in 1980 an adult rabbit tick, Haemaphysalis leporispalustris, taken from a black-tailed jack rabbit, Lepus californicus, in Mendocino County, California. In all examined biologic characteristics, this isolate, CA410, is indistinguishable from the prototype, strain 2678, isolated in Ontario, Canada, in 1963. These similarities include serologic and immunologic reactivity in laboratory mice and guinea pigs, cultural characteristics in Vero cells, chick embryo cells and embryonated eggs, low pathogenicity for mice, meadow voles and guinea pigs, unusual resistance to streptomycin, morphology by electron microscopy, and molar percentages of guanine plus cytosine of the deoxyribonucleic acids. Recovery of this second strain in the same species of tick, but far removed in time and place from the origin of the prototype, provides evidence that R. canada is an established, ecologically stable, rickettsia in North America.

Animals↗
PubMed1982

Survey for evidence of Colorado tick fever virus outside of the known endemic area in California.

A virus very similar or identical to Colorado tick fever (CTF) virus was recovered from the blood clot of one of 104 black-tailed jack rabbits (Lepus californicus) examined during a survey for various zoonotic agents in mammals and ticks from the University of California, Hopland Field Station, Mendocino County, California, 1974--79. This is the first reported isolation of a CTF-like virus from L. californicus, and only the second time such a virus has been found in northwestern California. Mendocino County is located far outside the known distributional ranges of the most common mammalian hosts of CTF virus and of Dermacentor andersoni, the only proven tick vector for man. The viral isolate is very similar to a CTF-like virus previously recovered from the blood and spleen of a western gray squirrel (Sciurus griseus) from San Luis Obispo County, an area also outside of the previously-known CTF area. Virus was not isolated from 14 additional species of mammals (354 specimens) or from eight species of ticks (4,487 individuals), but CTF-neutralizing antibodies were detected in 28 of 771 (3.6%) sera from seven of 15 mammalian species including significant titers (greater than or equal to 1:8) in two species and one subspecies not previously reported as natural hosts, i.e., brush mouse (Peromyscus boylii), pinyon mouse (P. truei), and Columbian black-tailed deer (Odocoileus hemionus columbianus). CTF indirect immunofluorescent antibodies also were detected in 26 of 129 (20.2%) sera belonging to four of five mammalian species tested. Neutralizing antibodies were found in sera of deer from other localities in Mendocino County, from a deer mouse from Napa County, and from a brush rabbit from Monterey County as well. These findings suggest that a virus identical or similar to CTF virus is widespread in northwestern-westcentral California, and that surveillance for human cases of CTF or a similar disease should be extended to cover this region.

Animals↗
PubMed1981

Serotypes of tick-borne spotted fever group rickettsiae from western California.

A rickettsial survey of ixodid ticks known to bite man was conducted in 1979 in four coastal counties of California to obtain isolates from tick species that might be involved in the transmission of spotted fever-like illnesses, and to examine serologic characteristics of the rickettsiae relative to defined members of the spotted fever group (SFG). One hundred and seventy (19.4%) of 877 ticks comprising three species were shown by hemolymph test to harbor rickettsia-like organisms. A total of 85 SFG rickettsia isolates was obtained by Vero-cell culture; 82 were from Dermacentor occidentalis, two were from D. variabilis, and one was from Ixodes pacificus. As determined by microimmunofluorescence, the isolates comprised four distinct serotypes. Two serotypes were obtained only from D. occidentalis, and one each only from D. variabilis and I. pacificus, respectively. Most D. occidentalis isolates possessed the serologic characteristics of Rickettsia rhipicephali, but there were similar to yet distinguishable from, R. rickettsii and are members of an unclassified serotype referred to as 364D. The two isolates from D. variabilis resembled the unclassified 369C serotype previously shown to be associated with this species and D. andersoni elsewhere in the United States. The I. pacificus isolate was similar to strains of the unclassified Tillamook serotype isolated from this tick in several localities in western Oregon. Representative strains of the four serotypes could also be distinguished on the basis of pathogenicity for Vero cells, chick embryos, guinea pigs, and/or meadow voles. The significance of these findings relative to occurrence of tick-associated illnesses in western California is briefly discussed.

California↗
PubMed1978

Effects of adenosine on intestinal hemodynamics, oxygen delivery, and capillary fluid exchange.

Systemic arterial pressure, superior mesenteric arterial and venous pressures, blood flow, arteriovenous oxygen difference, lymph flow, and intestinal volume were monitored continuously from an autoperfused loop of cat ileum to determine the effects of locally infused adenosine on intestinal hemodynamics, oxygen consumption, and capillary fluid exchange. The results indicate that adenosine, inosine, and hypoxanthine are vasodilators in the intestinal circulation. Local infusion of adenosine significantly reduces vascular resistance, but lymph flow, lymph oncotic pressure, and lymphatic protein flux remained unchanged from control, and the intestinal volume rapidly became constant after an initial blood volume shift. Intestinal oxygen consumption decreased significantly in both autoperfused and constant flow preparations. Pretreatment with aminophylline prevented the reduction in oxygen consumption and greatly attenuated the vasodilatory effect of adenosine. The reactive hyperemic response to 60-s arterial occlusions was virtually unchanged following aminophylline treatment. Adenosine depressed oxygen utilization of mucosal and muscularis strips in vitro and caused a significant redistribution of blood flow from the mucosal-submucosal layer to the muscularis in autoperfused preparations. The results of this study indicate that adenosine significantly reduces vascular resistance and oxygen consumption, yet does not alter fluid exchange in the small intestine.

Adenosine↗
PubMed1977

Sulfhydryl groups in relation to the structure and catalytic activity of 2-oxo-4-hydroxyglutarate aldolase from bovine liver.

Bovine liver 2-oxo-4-hydroxyglutarate aldolase (suggested name: 2-oxo-4-hydroxyglutarate glyoxylate-lyase catalyzing the reaction: 2-oxo-4-hydroxyglutarate in equilibrium pyruvate + glyoxylate) contains eight to ten sulfhydryl groups as determined by titration of the enzyme with either 5,5'-dithiobis(2-nitrobenzoic acid) (Nbs2) or p-mercuribenzoate in the presence of 1% sodium dodecyl sulfate. In the absence of a denaturant, all of the cysteinyl residues react with p-mercuribenzoate whereas only four are accessible to titration with Nbs2. No differences in -SH group reactivity can be detected during titration of the aldolase with p-mercuribenzoate. In contrast, two classes of sulfhydryls can be differentiated in the disulfide exchange reaction with Nbs2 in the absence of a denaturant; one -SH group (Class I) reacts rapidly whereas three additional thiols (Class II) titrate at approx. 0.1 the rate of the Class I-SH residue. Both pyruvate and glyoxylate protect one of the three -SH residues in Class II from reaction with Nbs2. Either substrate also prevents titration of one to two thiol groups by p-mercuribenzoate and decreases the rate of reaction of aldolase -SH groups with Nbs2 in 8 M urea. These ligand-induced changes in -SH reactivity provide a sensitive indication that the enzyme exists in an altered conformational state in the presence of either of its cosubstrates. Titration of the enzyme with either Nbs2 or p-mercuribenzoate results in a progressive loss of aldolase activity which is not proportional to the number of -SH groups modified. The enzyme retains 50% of the activity of the native enzyme when Class I and Class II thiols (i.e. four -SH groups total) are modified with Nbs2; 15% residual activity is still observed following titration of all of the cysteinyl residues with p-mercuribenzoate. Pyruvate and glyoxylate provide partial protection against inactivation. It is concluded that inactivation of 2-oxo-4-hydroxyglutarate aldolase by Nbs2 or p-mercuribenzoate is a consequence of alterations in protein structure which accompany modification of -SH groups. The data argue against the direct participation of an active-site thiol group in the catalytic mechanism of 2-oxo-4-hydroxyglutarate aldolase, be that aldol cleavage and condensation or beta-decarboxylation.

Aldehyde-Lyases↗
PubMed1976

Histidine decarboxylase of Lactobacillus 30a: function and reactivity of sulfhydryl groups.

Two classes of sulfhydryl groups in histidine decarboxylase from Lactobacillus 30 a can be differentiated by their reaction with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). Five cysteinyl residues (class I) of the native enzyme are titrated by DTNB as the pH of the reaction medium is increased from 6.5 to 7.5; the pH-rate profile for their reaction is described by a pKa of 9.2. An additional five thiol groups (class II) are titrated only when denaturing agents are added above neutral pH. Histidine decarboxylase is completely inactivated by DTNB in a kinetically second-order process (Kapp = 660 +/- 20 M-1 min-1 at pH 7.6 and 25 degrees C) which occurs coincident with and at the same rate as modification of the five class-I SH groups of the enzyme, i.e., one thiol group per pyruvoyl prosthetic group. The competitive inhibitors, histamine and imidazole, markedly enhanced the reactivity of these cysteinyl residues toward DTNB; this enhancement is accompanied by a concomitant increase in the rate of inactivation. A single SH group in each of the five catalytic units of histidine decarboxylase is thus implicated as being critical for the expression of enzymatic activity.

Binding Sites↗
PubMed1976

Histidine decarboxylase of Lactobacillus 30a: inactivation and active-site labeling by L-histidine methyl ester.

Histidine decarboxylase from Lactobacillus 30a is rapidly and irreversibly inactivated upon incubation with L-histidine methyl ester. The rate of inactivation is first-order with respect to remaining active enzyme and exhibits saturation kinetics with a kinact of 1.2 mM and an apparent first-order rate constant of 0.346 min-1 at pH 4.8 and 25 degrees C. On complete inactivation, 3 mol of [14C]histidine (from L-[14C]histidine methyl ester) and 2 mol of 14C (from L-histidine [14C]methyl ester) are bound in nondialyzable form per mol (190 000 g) of protein inactivated with a corresponding loss of three of the five DTNB-titratable--SH groups that are essential for activity of the native enzyme. Imidazole propionate, a competitive inhibitor of the enzyme, protects against inactivation, loss of --SH groups, and incorporation of radioactivity from both the histidine and the methyl ester moieties of the labeled inhibitor, and kinetic evidence indicates that imidazole propionate and histidine methyl ester compete for binding at the active site of histidine decarboxylase in a mutually exclusive manner. Treatment of the labeled protein with either alkali or hydroxylamine results in the quantitative release of radioactivity. These data suggest that inactivation of histidine decarboxylase by L-histidine methyl ester results from two different modes of interaction between the inhibitor and the active site of histidine decarboxylase; the major interaction involves an essential -SH group.

Binding Sites↗
PubMed1975

Differences between human Fe1-transferrin molecules.

Two molecular forms of Fe1-transferrin molecule can be demonstrated by anion-exchange chromatography on columns of DEAE-cellulose, pH 7.90. It is believed that co-ordination of each metal-binding site by ferric ions induces dissimilar changes in molecular conformation in the region of the binding sites which, in the case of one site, results in the molecule behaving as a weaker anion during anion-exchange chromatography. If so, this could be entirely in accord with current views that the two binding sites of transferrin do not share equal properties of iron exchange with cells. At physiological levels of transferrin iron-saturation, it is likely that two populations of Fe1-transferrin molecules form the bulk of the iron-transferrin complex.

Binding Sites↗