Ferenc J. Kezdy

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The cytotoxic peptide from honeybee venom, melittin, and a synthetic peptide analogue of it lyse human erythrocytes in a biphasic process. The kinetics of the lysis in 0.30 M sucrose, 0.01 M sodium phosphate, pH 7.30 at 4 degrees C were investigated. Our results show that melittin rapidly binds to the outer surface of the erythrocyte membrane, and the(More)
Statistical analysis of an expanded data base of regions in viral polyproteins and in non-viral proteins that are sensitive to hydrolysis by the protease from human immunodeficiency virus (HIV) type 1 has generated a model which characterizes the substrate specificity of this retroviral enzyme. The model leads to an algorithm for predicting(More)
A calcium oxalate monohydrate crystal growth inhibitor has been isolated from human kidney tissue culture medium by using DEAE-cellulose batch chromatography followed by DEAE-cellulose and Sephacryl S-200 chromatography. The isolated inhibitor was found to be a glycoprotein with a M, = 1.33 X lo4, as determined by analytical ultracentrifugation, and a(More)
The acceptor substrate specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) was inferred from the amino acid sequences surrounding 196 O-glycosylation sites extracted from the National Biomedical Research Foundation Protein Database. When analyzed according to the cumulative enzyme specificity model (Poorman, R.A.,(More)
The behavior of multilamellar liposomes of 2,3-dipalmitoyl-sn-glycero-1-phosphocholine (DPPC) was studied by differential scanning calorimetry (DSC) in the presence of < or = 5 mol % of the amphiphilic solutes methyl oleate, cholesterol, pregnenolone, and dehydroandrosterone. The DSC thermograms indicate that the solutes are miscible only with the(More)
Human immunodeficiency virus 1 (HIV-1) protease is an aspartyl protease composed of two identical protomers linked by a four-stranded antiparallel beta-sheet consisting of the NH2- and COOH-terminal segments (Weber, I.T. (1990) J. Biol. Chem. 265, 10492-10496). Kinetic analysis of the HIV-1 protease-catalyzed hydrolysis of a fluorogenic substrate(More)
Using an assay of the rate of crystal growth of calcium [14C]oxalate monohydrate, we ascertained that the factor responsible for more than 90% of the crystal growth inhibition in human urine is a nondialyzable macromolecule. We have purified this factor using DEAE-cellulose chromatography, followed by Bio-Gel P-10 column chromatography with 50% formamide as(More)
Two major outer envelope glycoproteins of Epstein-Barr virus, gp350 and gp220, are known to be encoded by 3.2- and 2.5-kilobase RNAs which map to the same DNA fragment (M. Hummel, D. Thorley-Lawson, and E. Kieff, J. Virol. 49:413-417). These RNAs have the same 5' and 3' ends. The larger RNA is encoded by a 2,777-base DNA segment which is preceded by(More)
cis-Parinaric acid (PnA), cis-trans-trans-cis-9, 11, 13, 15-octadecatetraenoic acid, is fluorescent (epsilon = 74,000 at 324 nm) when partitioned into a lipid environment and the fluorescence is destroyed upon reaction with free radicals. It has been used to monitor semiquantitatively free-radical-induced lipid peroxidation in human erythrocyte membranes.(More)
Mucin type O-glycosylation begins with the transfer of GalNAc to serine and threonine residues on proteins by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminlytransferases. These enzymes all contain a lectin-like (QXW)(3) repeat sequence at the C terminus that consists of three tandem repeats (alpha, beta, and gamma). The putative lectin domain of(More)