Adenoid cystic carcinoma of minor salivary glands.
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Adult↗
Biomedical subjects
D Man
Publications and source records attributed to D Man.
Immunological, structural and functional relationships between an anti-complementary protein from Crotalus atrox venom, cobra venom factor and human C3.
An anti-complementary protein which cross-reacts with antiserum to cobra venom factor (CoF) has been highly purified from Crotalus atrox venom (CAV). On an equal weight basis, the C. atrox factor (CA-F) had one-third the anti-complementary activity of CoF and similarly consumed the terminal components of complement via the alternative pathway. The subunit compositions of CoF and CAV were similar, each being composed of alpha and beta chains held together by covalent and non-covalent bonds. Agarose gel diffusion analysis using monospecific antiserum to CoF detected a reaction of partial immunological identity between CoF and CA-F and between C3 and CA-F with the CoF and C3 precipitin lines spurring over the CA-F lines. Thus CA-F probably represents a C. atrox C3 protein which is capable of activating the alternative complement pathway via the amplification loop in a manner analogous to that of C3b and CoF.
Animals↗
Kinetic studies on the fragmentation of the third component of complement (C3) by trypsin.
The kinetics of cleavage of C3 by trypsin was analyzed by electrophoresis in agarose and in polyacrylamide gels containing sodium dodecyl sulfate and the data obtained were used to construct an anatomical model for C3 showing the sites of tryptic attack, the fragments generated, and their composition. Trypsin was shown to cleave C3 in a stepwise fashion. The attack was initially directed at the alpha-polypeptide chain and resulted in the generation of C3a and C3b. Further cleavage of the alpha-chain of C3b, converted it into C3b1 and then into C3d and C3c. Cleavage of the beta-chain by trypsin occurred only at the C3c stage with the release of a small peptide (m.w. 12,000) from C3c and the formation of C3c'. On immunoelectrophoresis, C3c' had a less anodal mobility compared to the beta1A mobility of C3c. C3a, once formed could be further cleaved to give residual fragments with decreasing net positive charge. Exposure of C3 to acid conditions, pH 5.0 or below, rendered the molecule exceedingly susceptible to tryptic degradation.
Citrates↗
Bimodal effect of amphiphilic biocide concentrations on fluidity of lipid membranes.
Using the spin label method (ESR) it has been shown that biologically active, amphiphilic compounds (quaternary ammonium salts (AS) containing polar heads with single and double positive charge caused, at low concentrations, decrease fluidity of liposome membranes formed with egg yolk lecithin (EYL). At higher concentrations an increase in fluidity was observed. With compounds having a single positive charge minimum fluidity of membrane structure occurs in the range of 1 to 3%, with compounds containing double positive charge-in the range of 4-6%. That effect does not depend on polar head size and length of alkyl chains of the AS used. Analysis of the electrostatic interaction between positive charges and dipole system suggest that at low ion concentrations the binding energy of the system increases, while it decreases at high concentrations. For the model presented, maximum of binding energy of the system occurs at 3% of positive monovalent ions and at 6% of positive divalent ions admixed.
Cyclic N-Oxides↗
ESR study of the liposome membrane physical parameters in the heating-cooling cycles.
Changes of dynamic and structural parameters of egg yolk lecithin (EYL) liposome membranes in the heating-cooling cycles have been studied using the ESR spin probe method. The investigations were conducted in the range of temperatures from -18 degrees C to +60 degrees C. It has been found that in the range of temperatures -15 degrees C to +45 degrees C in both the heating and the cooling run the spectroscopic parameters changed practically along the same curve (reversible changes). However, after exceeding this range of temperatures one of the parameters (partition coefficient of the spin probe 2,2,6,6--tetramethylpiperidine -1-oxyl; TEMPO) changed along a closed curve, showing the phenomenon of thermal hysteresis. In the heating process the TEMPO content in liposome membranes was smaller than this in the cooling process. We assume that during the heating, the lipid molecules of the outer liposome layers dissolve in the aqueous medium. In the cooling process they can aggregate and form new liposomes, what in turn increases the surface of liposome membranes, accessible for the TEMPO probe (active surface).
Cold Temperature↗
Computer simulations of the electric interactions between the phospholipid head-groups and ionic admixtures in the membrane surface.
Some phospholipids (e.g. lecithin) form a system of electric dipoles on the membrane surface layer. In the case of lecithin the positive dipole charge is located on the choline and the negative one on the phosphoric molecule group. These dipoles are arranged almost parallel to the membrane surface. Taking the dipole membrane structure as a base for further investigations, a computer model of the electrostatic interaction between the dipole system and the ionic admixture was investigated. The model presumes hexagonal centered or a rectangular flat geometry of the 121 dipoles distribution. The dipoles may rotate freely around round the motionless symmetry axis perpendicular to the system surface. The initial state is given by fixing the geometry of the dipole matrix and ionic admixture distribution. Subsequently this system underwent a computer simulation which consisted of a calculation of resultant force moments acting on each dipole caused by other dipoles and ions. These force moments lead the system to the equilibrium state (minimum of the binding energy). The minimum energy value of the dipoles system depends on concentration and charge of the admixtured ions. The results of repeated simulations indicate that the system achieve the least of all binding energy (the most stable equilibrium state) at 1.5% concentration of admixtured ions in case of ion charge equal to 1Q (where Q denotes arbitrary unit of ion charge) and at 2.5% concentration of admixtured ions in case of ion charge equal to 2Q. The calculated results are in a good agreement with the experimental.
Computer Simulation↗
Drug allergy: incidence in terms of age and some drug allergens.
The authors studied the incidence of drug allergy in 3 groups of subjects. In the first group the incidence was established in terms of the subjects' age: 1.8% in children up to 14 years old (323 subjects), 5.8% in middle-aged subjects (389 subjects) and 2.9% in the elderly (243 subjects). In the second partly selected group, drug allergy was studied in patients admitted to the 3rd Medical Clinic--Craiova between 2 Jan. 1981 and 31 Dec. 1982; 103 of the 8,760 patients admitted presented allergic reactions, a relatively high incidence rate (1.01%) as compared to other published reports. The third group of previously selected cases consisted of 197 patients who had come to the allergology service with complaints of present or past sensitivity to drugs. The total number of patients was 336 selected or preselected from about 10,000 subjects, to which 17 patients with a diagnosis of "asthmatic triad" must be added. Drug allergy in terms of the drug used was dominated by penicillin, pyramidon-algocalmin, aspirin, iodine preparations, etc.; foremost among the clinical syndrome were the dermatologic syndromes types I, III and IV; syndromes of the "anaphylactic shock" type, "serum sickeness" bronchial asthma, angioneurotic oedema.
Adolescent↗