D.J. Strydom

The amino-terminal sequence of silk fibroin peptide CP - a reinvestigation.

Abstract A new amino-acid sequence is proposed for silk fibroin peptide Cp, after automatic Edman degradation studies. The proposed sequence is: Gly-Ala-Gly-Ala-Gly-Ser-Gly-Ala-Ala-Gly-(Ser-Gly-(Ala-Gly) n ) 8 Tyr, where n is usually 2.

Snake venom toxins—I. Preliminary studies on the separation of toxins of elapidae venoms

Abstract The venoms of nine Elapidae snakes representing three genera were fractionated by chromatography on Amberlite CG-50 and Sephadex G-50 and the elution positions of their toxins determined. Two or more distinct toxins were contained in each of these venoms. A very low molecular weight toxic component was found in Naja naja and two of the three Dendroaspis venoms. Its molecular weight is estimated at 3000–4000, i.e. nearly half the size of the toxins usually found in front fanged snakes. Dendroaspis angusticeps venom contained only biologically deleterious components which failed to kill mice although the whole venom is highly toxic. It is possible that a combination of fractions from this venom is necessary for its lethal action.

Snake venom toxins The amino acid sequence of toxin vi2, a homologue of pancreatic trypsin inhibitor, from dendroaspis polylepis polylepis (black mamba) venom

The amino acid sequence of venom component Vi2, a protein of low toxicity from Dendroaspis polylepis polylepis venom was determined by automatic sequence analysis in combination with sequence studies on tryptic peptides. This protein, the most retarded fraction of this venom on a cation-exchange resin, is a homologue of bovine pancreatic trypsin inhibitor consisting of a single chain of 57 amino acid residues containing six half-cystine residues. The active site lysyl residue of bovine trypsin inhibitor is conserved in Vi2 although large differences are found in the rest of the molecule.

Phylogenetic relationships of proteroglyphae toxins.

Abstract The amino acid sequences of eleven Proteroglyphae toxins were used in setting up a phylogenetic relationship between these toxins. A probable sequence of genetic events leading to this relationship is postulated.

Homology of functionally diverse proteins.

SummaryDisulphide-rich proteins of widely differing functions were aligned with the aid of their half-cystinyl residues. This led to the grouping of ribonuclease, phospholipase A, lysozyme, snake venom toxins, bee and scorpion venom peptides, and the plant proteins potatoe carboxypeptidase inhibitor, ragweed pollen allergen, mistletoe toxins and pineapple sulfhydryl protease inhibitor into one super-family of proteins. Very few deletions/insertions were needed to effect alignment and probabilities were calculated for random occurrence of the matches that were found.

The amino acid sequence of ostrich (Struthio camelus) cytochrome c

1. 1. The amino acid sequence of Struthio camelus cytochrome c was derived by sequencing tryptic peptides. 2. 2. The sequence differs from that of the typical bird cytochrome c in a single position. 3. 3. Phylogenetic studies were carried out to compare the positioning of chicken, turkey, Pekin duck, penguin, pigeon and ostrich according to their cytochrome c structures.