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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)
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)
Previous studies point to the acidic amino-terminal segment of band 3, the anion transport protein of the red cell, as the common binding site for hemoglobin and several of the glycolytic enzymes to the erythrocyte membrane. We now report on the interaction of hemoglobin with the synthetic peptide AcM-E-E-L-Q-D-D-Y-E-D-E, corresponding to the first 11(More)
The synthetic nonapeptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val is a substrate for in vitro phosphorylation by a partially purified preparation of rat brain protein kinase C, with Kmapp of about 130 microM. The closely related peptide kemptide was a much weaker substrate, bovine serum albumin was not a substrate and the peptide(More)
Bacterial signal peptides display little amino acid sequence homology despite their shared role in mediating protein transport. This heterogeneity may exist to permit the establishment of signal peptide conformations that are appropriate for transport of particular proteins. In this paper we explore how signal peptides are composed of structural units that(More)
A 29-amino acid analog of growth hormone releasing factor (GHRF) was designed in which the sequence of the first six amino acids at the amino terminus was maintained while the postulated amphiphilic helical structure in the remainder of the molecule was optimized. The amino acid sequence of the analog differed from that of the first 29 residues of human(More)