scholarly journals Immunochemical cross-reactivity between cyanogen bromide fragments of human serum albumin.

1982 ◽  
Vol 257 (6) ◽  
pp. 2770-2774
Author(s):  
N Doyen ◽  
A J Pesce ◽  
C Lapresle
1993 ◽  
Vol 639 (2) ◽  
pp. 341-345 ◽  
Author(s):  
Anna Compagnini ◽  
Maria Fichera ◽  
Salvatore Fisichella ◽  
Salvatore Foti ◽  
Rosaria Saletti

1979 ◽  
Vol 177 (1) ◽  
pp. 251-254 ◽  
Author(s):  
N Doyen ◽  
C Lapresle

When human albumin was treated with CNBr, a fragment designated D was obtained and attributed to the absence from some of the albumin molecules of methionine at position 123 [Lapresle & Doyen (1975) Biochem. J. 151, 637-643]. The present study shows that methionine-123 is converted into homoserine without cleavage of the subsequent methionine-cystine bond. With bovine alpha-lactalbumin, a further example of non-cleavage of a methionine-cystine bond with conversion of methionine into homoserine is reported.


1979 ◽  
Vol 44 (5) ◽  
pp. 1657-1670 ◽  
Author(s):  
Ladislav Morávek ◽  
Mohamed Ali Saber ◽  
Bedřich Meloun

Human serum albumin was nitrated by an excess of tetranitromethane at pH 8.0. As shown by amino acid analysis, of the 18 tyrosine residues present in albumin about 7-7.5 residues remain unaltered, 9 residues are converted into 3-nitrotyrosine, and 1.2 residue into 3,5-dinitrotyrosine. The nitrated albumin was digested with cyanogen bromide to three fragments which comprise the whole original molecule. The individual fragments were converted into their S-sulfo derivatives and the latter digested with chymotrypsin or stepwise with trypsin and thermolysin. The yellow, nitrotyrosine-containing peptides were isolated from the digest and the positions of nitrated tyrosine residues in albumin thus located. Residues No 30, 148, 150, 161, 334, 341, 401, and 411 were identified as strongly nitrated and residues No 84, 138, 452, and 497 as medium nitrated. Residues No 140, 263, 319, 332, 353, and 367 either react weakly or were not found in nitrated form. Residue No 411 and partly also 161 were converted into 3,5-dinitrotyrosine. The accessibility of the individual tyrosine residues to the nitrating agent is discussed with respect to their positions in disulfide loops and hypothetic parts of the secondary structure of albumin.


2002 ◽  
Vol 83 (4) ◽  
pp. 2248-2258 ◽  
Author(s):  
Enrico Monzani ◽  
Maria Curto ◽  
Monica Galliano ◽  
Lorenzo Minchiotti ◽  
Silvio Aime ◽  
...  

1971 ◽  
Vol 246 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
Rapier H. McMenamy ◽  
Howard M. Dintzis ◽  
Frank Watson

1978 ◽  
Vol 9 (5) ◽  
pp. 349-355 ◽  
Author(s):  
Z. Hrkal ◽  
M. Kodíček ◽  
Z. VodrÁžka ◽  
B. Meloun ◽  
L. Morávek

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