EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

The primary structure of human erythrocyte copper zinc super oxide dis mutase cleavage with staphylococcus aureus protease determination of the amino terminal blocking group and location of the di sulfide bond






Italian Journal of Biochemistry (English Edition) 31(1): 39-48

The primary structure of human erythrocyte copper zinc super oxide dis mutase cleavage with staphylococcus aureus protease determination of the amino terminal blocking group and location of the di sulfide bond

Results obtained after digestion of copper/zinc superoxide dismutase from human erythrocytes with S. aureus protease are described. Peptides soluble in alkaline conditions were essential for completing the determination of the primary structure of the enzyme; other peptides were important for establishing the amidation state of dicarboxylic amino acid residues and for confirming controversial sequences. The human enzyme was acetylated at the NH2 terminus and contained an intrasubunit disulfide bond connecting half-cystine residues 57 and 146.


Accession: 006740918



Related references

Martini, F.; SchininĂ , M.E.; Bannister, W.H.; Bannister, J.V.; Barra, D.; Rotilio, G.; Bossa, F., 1982: The primary structure of human erythrocyte copper/zinc superoxide dismutase: cleavage with Staphylococcus aureus protease, determination of the N-terminal blocking group and location of the disulfide bond. Results obtained after digestion of copper/zinc superoxide dismutase from human erythrocytes with S. aureus protease are described. In particular, peptides soluble in alkaline conditions proved essential for completing the determination of the pri...

Barra, D.; Martini, F.; Bannister, W.H.; Bannister, J.V.; Rotilio, G.; Bossa, F., 1982: The primary structure of human erythrocyte copper zinc super oxide dis mutase ec 1.15.1.1 cleavage with trypsin and chymotrypsin. Results obtained after digestion of copper/zinc superoxide dismutase from human erythrocytes with trypsin and chymotrypsin are described. Tryptic digestion produced a relatively simple mixture of soluble peptides, which were purified and analyzed...

Steffens, G.J.; Bannister, J.V.; Bannister, W.H.; Flohe, L.; Guenzler, W.A.; Kim, S.M.A.; Oetting, F., 1983: The primary structure of copper zinc super oxide dis mutase ec 1.15.1.1 from photobacterium leiognathi evidence for a separate evolution of copper zinc super oxide dis mutase in bacteria. The complete amino-acid sequence of the copper-zinc superoxide dismutase of the P. leiognathi was determined. The fragmentation strategy employed included cyanogen bromide cleavage at its Met residues and the only Try residue. The S-carboxymethyla...

Bauer R.; Demeter I.; Hasemann V.; Johansen J.T., 1980: Structural properties of the zinc site in copper zinc super oxide dis mutase perturbed angular correlation of gamma ray spectroscopy on the copper cadmium 111 super oxide dis mutase derivative. The Zn(II) site of the dimeric Cu(II),Zn(II)-superoxide dismutase from Saccharomyces cerevisiae was examined by perturbed angular correlation of .gamma.-rays (PAC) on the Cu(II),Cd(II)- and Cu(I),Cd(II)-superoxide dismutase. The PAC spectrum for t...

Crosti N.; Bajer J.; Rigo A.; Serra A.; Viglino P.; Argese E.; Mavelli I., 1983: Manganese super oxide dis mutase copper zinc super oxide dis mutase glutathione per oxidase and catalase activities in human fibroblasts in vitro. Acta Medica Romana 21(3): 458-463

Stallings W.; Bull C.; Pattridge K.A.; Powers T.B.; Fee J.A.; Ludwig M.L.; Ringe D.; Petsko G.A., 1984: The 3 dimensional structure of iron super oxide dis mutase kinetic and structural comparisons with copper zinc dis mutase and manganese dis mutase. Bors, W , M Saran And D Tait (Ed ) Oxygen Radicals in Chemistry And Biology; Proceedings Of The 3rd International Conference, Neuherberg, West Germany, July 10-15, 1983 Xix+1029p Walter De Gruyter: Berlin, West Germany; New York, N Y , Usa Illus P779-792

Tainer J.A.; Getzoff E.D.; Beem K.M.; Richardson J.S.; Richardson D.C., 1982: Determination and analysis of the 2 angstrom structure of copper zinc super oxide dis mutase. The structure of bovine erythrocyte Cu,Zn superoxide dismutase was determined to 2 .ANG. resolution using only the larger structure factors beyond 4 .ANG. The enzyme crystallizes in space group C2 with 2 dimeric enzyme molecules/asymmetric unit. A...

Westman, N.G.; Marklund, S.L., 1981: Copper containing and zinc containing super oxide dis mutase and manganese containing super oxide dis mutase ec 1.15.1.1 in human tissues and human malignant tumors. Superoxide dismutases might protect against ionizing radiation and free radical-producing antibiotic antitumor drugs. Copper- and zinc-containing superoxide dismutase (CuZn superoxide dismutase) and manganese-containing superoxide dismutase (Mn su...

Marklund S.L.; Westman N.G.; Lundgren E.; Roos G., 1982: Copper containing and zinc containing super oxide dis mutase manganese containing super oxide dis mutase catalase and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues. Copper- and zinc-containing superoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase form the primary enzymic defense against toxic oxygen reduction metabolites. Such metabolites have been implicated in...

Gaertner A.; Leippert M.; Weser U., 1984: Erythrocuprein copper zinc super oxide dis mutase carries 90 percent of the erythrocyte copper. Bors, W , M Saran And D Tait (Ed ) Oxygen Radicals in Chemistry And Biology; Proceedings Of The 3rd International Conference, Neuherberg, West Germany, July 10-15, 1983 Xix+1029p Walter De Gruyter: Berlin, West Germany; New York, N Y , Usa Illus P803-808