Purification, N-Terminal Amino Acid Sequence and Partial Characterization of A Cu,Zn Superoxide Dismutase From the Pathogenic FungusAspergillusfumiga Tus

1995 ◽  
Vol 22 (6) ◽  
pp. 519-531 ◽  
Author(s):  
M. D. Holdom ◽  
R. J. Hay ◽  
A. J. Hamilton
Keyword(s):  
Superoxide Dismutase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Characterization ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

scholarly journals Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits

2003 ◽  
Vol 15 (2) ◽  
pp. 119-122 ◽  
Author(s):  
Marli Lourdes de Oliveira ◽  
Leila Maria Beltramini ◽  
Salvatore Giovanni de Simone ◽  
Maria Helena Nasser Brumano ◽  
Rosemeire Aparecida Silva-Lucca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Amino Acid ◽  
Saline Extract ◽  
Hydrophobic Residues ◽  
Terminal Amino ◽  
Helix Conformation ◽  
Far Ultraviolet ◽  
Terminal Amino Acid Sequence

A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).

scholarly journals The preparation and partial characterization of N-terminal and C-terminal iron-binding fragments from rabbit serum transferrin

1982 ◽  
Vol 205 (3) ◽  
pp. 611-617 ◽  
Author(s):  
S Heaphy ◽  
J Williams
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rabbit Serum ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Terminal Amino Acid ◽  
Terminal Domain ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Two iron-binding fragments of Mr 36 000 and 33 000 corresponding to the N-terminal domain of rabbit serum transferrin were prepared. One iron-binding fragment of Mr 39 000 corresponding to the C-terminal domain was prepared. The N-terminal amino acid sequence of rabbit serum transferrin is: Val-Thr-Glu-Lys-Thr-Val-Asn-Trp-?-Ala-Val-Ser. One glycan unit is presented in rabbit serum transferrin and it is located in the C-terminal domain.

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