ABSTRACT
The polypeptide sequence of the unmodified catalase from Penicillium vitale containing 696 amino acid residues was deduced. The sequences of 76 tryptic peptides of the unmodified catalase, 63 tryptic peptides of the catalase with modified Lys residues, 48 peptides resulting from catalase cleavage by the Staphylococcus aureus V8 protease, and 9 fragments obtained by BrCN-treatment were considered, and a comparison with the sequences of other catalases was made.
Subject(s)
Catalase/chemistry , Penicillium/enzymology , Amino Acid Sequence , Chromatography, High Pressure Liquid , Cyanogen Bromide/chemistry , Endopeptidases/chemistry , Lysine/chemistry , Molecular Sequence Data , Peptide Fragments/chemistry , Sequence Homology, Amino Acid , Staphylococcus aureus/enzymologyABSTRACT
The amino acid sequence of Agrotis segetum Granulosis virus (AsGV) granulin and A. Segetum nuclear polyhedrosis virus (AsNPV) polyhedrin was determined by sequencing tryptic and chymotryptic peptides from reduced and carboxymethylated proteins and tryptic fragments of oxidized and maleylated granulin. The comparison of the established peptide structures with the primary structures of other occlusion body proteins from related baculoviruses was also used for the polypeptide chains' reconstruction. The polypeptide chains of AsGV granulin and AsNPV polyhedrin comprise 247 and 246 amino acid residues, respectively. The proteins possess a high percentage of homology in their primary structures (63%).
Subject(s)
Baculoviridae/chemistry , Inclusion Bodies, Viral/chemistry , Moths/microbiology , Amino Acid Sequence , Animals , Molecular Sequence Data , Occlusion Body Matrix Proteins , Peptide Fragments/chemistry , Sequence Homology, Nucleic Acid , Viral Structural ProteinsABSTRACT
A molecule of Penicillium vitale catalase is shown to dissociate into subunits with the molecular weight 75-80 kDalton. When hemin is splitted off the molecule also disintegrates into subunits equalling 1/4 of the enzyme molecule. The amino acid composition and fingerprints of the catalase subunits were studied. It is supposed that N-terminal residue of the subunit is blocked.
Subject(s)
Catalase/analysis , Penicillium/enzymology , Amino Acid Sequence , Catalase/isolation & purification , Electrophoresis, Polyacrylamide Gel , Hydrolysis , Molecular Weight , Protein ConformationABSTRACT
Using disc polyacrylamide gel electrophoresis, the molecular weights of polyhedral proteins of nuclear polyhedrosis viruses (NPV) of Porthetria dispar, Mamestra brassicae, and Aporia crataegi were found to be 28000 +/- 3000. It was shown that NPV polyhedra of Bombyx mori, Galleria mellonella, P. dispar, and M. brassicae contain a protease. During dissolution of the polyhedra at pH 10,5 this protease specifically cleaves the matrix protein into 2--5 fragments. The amino acid compositions of NPV polyhedral proteins of P. dispar, M. brassicae, A. crataegi, Hyphantria cunae were shown to be very similar. It was found that tyrosine is a C-terminal amino acid of NPV polyhedral proteins of P. dispar, M. brassicae, and A. crataegi.
Subject(s)
Insect Viruses/analysis , Viral Proteins , Humans , Hydrogen-Ion Concentration , Insecta , Macromolecular Substances , Molecular Weight , Species Specificity , Viral Proteins/isolation & purificationABSTRACT
Amino acid composition, partial or complete sequence of 43 tryptic peptides of pelyhedral protein of nuclear polyhedrosis virus is investigated. These peptides include 327 amino acid residues. There are 28 peptides with unique sequences containing 240 amino acid residues. It conforms to polypeptide chain molecular weight ca. 28000 and coincides with earlier reported data on polyacrylamide gel electrophoresis.
