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Chemical conversion of aspartic acid 52, a catalytic residue in hen egg white lysozyme, to homoserine
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Year:
1974
Source of publication :
Proceedings of the National Academy of Sciences of the United States of America
Authors :
Eshdat, Yuval
;
.
Volume :
71
Co-Authors:
Eshdat, Y., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Dunn, A., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Sharon, N., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Facilitators :
From page:
1658
To page:
1662
(
Total pages:
5
)
Link :
Chemical conversion of aspartic acid 52, a catalytic residue in hen egg white lysozyme, to homoserine
Abstract:
[No abstract available]
Note:
Related Files :
Animal
catalysis
chemistry
Chickens
egg white
Esters
lysozyme
Ovalbumin
tritium
Show More
Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
25307
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:13
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Scientific Publication
Chemical conversion of aspartic acid 52, a catalytic residue in hen egg white lysozyme, to homoserine
71
Eshdat, Y., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Dunn, A., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Sharon, N., Dept. Biophys., Weizmann Inst. Sci., Rehovot, Israel
Chemical conversion of aspartic acid 52, a catalytic residue in hen egg white lysozyme, to homoserine
[No abstract available]
Scientific Publication
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