Study of the influence of chemical modification of the tryptophan residues in the molecules ofDatura innoxia lectins on their hemagglutinating activity

1997 ◽  
Vol 33 (5) ◽  
pp. 574-577
Author(s):  
S. V. Levitskaya ◽  
T. S. Yunusov
Keyword(s):  
Chemical Modification ◽  
Hemagglutinating Activity ◽  
Tryptophan Residues

Studies of Glutamate Dehydrogenase: Chemical Modification and Quantitative Determination of Tryptophan Residues

1974 ◽  
Vol 43 (2) ◽  
pp. 319-325 ◽  
Author(s):  
Veit Witzemann ◽  
Rudolf Koberstein ◽  
Horst Sund ◽  
Ihab Rasched ◽  
Hans Jornvall ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Quantitative Determination ◽  
Glutamate Dehydrogenase ◽  
Tryptophan Residues

scholarly journals Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification

1996 ◽  
Vol 5 (11) ◽  
pp. 2311-2318 ◽  
Author(s):  
Mark R. Bray ◽  
Neil R. Gilkes ◽  
Douglas G. Kilburn ◽  
R. Antony J. Warren ◽  
Lawrence P. Mcintosh ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Tryptophan Residues ◽  
Cellulose Binding

Chemical modification of tryptophan residues and stability changes in proteins

Biochemistry ◽  
1990 ◽  
Vol 29 (39) ◽  
pp. 9168-9175 ◽  
Author(s):  
Toshihide Okajima ◽  
Yasushi Kawata ◽  
Kozo Hamaguchi
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residues

Chemical modification of tryptophan residues in castor bean hemagglutinin.

1985 ◽  
Vol 49 (11) ◽  
pp. 3301-3308 ◽  
Author(s):  
Nobuyuki YAMASAKI ◽  
Nural ABSAR ◽  
Gunki FUNATSU
Keyword(s):  
Chemical Modification ◽  
Castor Bean ◽  
Tryptophan Residues

Chemical Modification of Tryptophan Residues in Castor Bean Hemagglutinin

1985 ◽  
Vol 49 (11) ◽  
pp. 3301-3308
Author(s):  
Nobuyuki Yamasaki ◽  
Nural Absar ◽  
Gunki Funatsu
Keyword(s):  
Chemical Modification ◽  
Castor Bean ◽  
Tryptophan Residues

Influence of Tryptophan Modification upon Digestion of Antithrombin III by Elastase

1991 ◽  
Vol 65 (04) ◽  
pp. 351-354 ◽  
Author(s):  
M F Scully ◽  
N Shah ◽  
V Ellis ◽  
V V Kakkar
Keyword(s):  
Molecular Weight ◽  
Chemical Modification ◽  
Neutrophil Elastase ◽  
Antithrombin Iii ◽  
High Affinity ◽  
Tryptophan Residues ◽  
Tryptophan Modification ◽  
Modified Forms ◽  
Molecular Weight Form

SummaryChemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Upon digestion with pancreatic or neutrophil elastase the low affinity forms generate a product of molecular weight form (55 kDa) not seen in digests of native antithrombin III or modified forms with high affinity for heparin. When measured as loss of activity the obserued rate of digestion of the latter in the absence of heparin was more rapid than that of native antithrombin III. The differences in digestion are considered to be related to conformation at differences between the various forms.

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