Primary structure of a guanyl-specific ribonuclease from the fungus Penicillium brevicompactum

Journal Article · Wed Jan 01 04:00:00 EST 1986 · Sov. J. Bioorg. Chem. (Engl. Transl.); (United States)

OSTI ID:5244017

Kulikov, V A; Shlyapnikov, S V; Yakovlev, G I

By the automatic Edman degradation of the intact S-carboxymethylated protein and a mixture of the products of its proteolytic cleavage at Arg, Lys, and Glu residues, together with results on the kinetics of the proteolysis of the protein under the action of carboxypeptidase Y, the primary structure of the extracellular guanyl-specific RNase of the fungus Penicillium brevicompactum has been determined. The RNase contains 102 amino acid residues: 7 Asp, 7 Asn, 9 Thr, 11 Ser, 4 Glu, 1 Gln, 4 Pro, 10 Gly, 11 Ala, 4 Cys, 7 Val, 4 Ile, 3 Leu, 9 Tyr, 5 Phe, 2 Lys, 3 His, 1 Arg (M/sub r/ 10,801). It has been established that four hemicystine residues of the P. compactum RNase form, in pairs, two disulfide bonds

• Research Organization: Institute of Molecular Biology, Moscow (USSR)
• OSTI ID: 5244017
• Journal Information: Sov. J. Bioorg. Chem. (Engl. Transl.); (United States), Journal Name: Sov. J. Bioorg. Chem. (Engl. Transl.); (United States) Vol. 11:3; ISSN SJBCD
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
BACTERIA
BIOCHEMICAL REACTION KINETICS
CARBON 14 COMPOUNDS
CARBOXYPEPTIDASES
CHEMICAL REACTIONS
COUNTING TECHNIQUES
DECOMPOSITION
ENZYMATIC HYDROLYSIS
ENZYME ACTIVITY
ENZYMES
ESTERASES
FUNGI
GUANYLIC ACID
HYDROLASES
HYDROLYSIS
ISOTHIOCYANATES
KINETICS
LABELLED COMPOUNDS
LABELLING
LYSIS
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PENICILLIUM
PEPTIDE HYDROLASES
PHOSPHODIESTERASES
PLANTS
PROTEINS
PROTEOLYSIS
RADIOENZYMATIC ASSAY
REACTION KINETICS
RNA-ASE
SCINTILLATION COUNTING
SERINE PROTEINASES
SOLVOLYSIS
STAPHYLOCOCCUS
TRYPSIN