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פותח על ידי קלירמאש פתרונות בע"מ -
Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme
Year:
1973
Source of publication :
Journal of Biological Chemistry
Authors :
אשדת, יובל
;
.
Volume :
248
Co-Authors:
Eshdat, Y., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
McKelvy, J.F., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
Sharon, N., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
Facilitators :
From page:
5892
To page:
5898
(
Total pages:
7
)
Abstract:
Hen egg white lysozyme, fully inactivated by the affinity labeling reagent, the 2',3' epoxypropyl β glycoside of di (N acetyl D glucosamine), contained 1 mole of the label per mole of protein. Total enzymatic digestion of the reduced and carboxymethylated affinity labeled enzyme afforded, as a major radioactive product, a compound composed solely of aspartic acid and glucosamine at the molar ratio of 1:2. Peptic digestion afforded a single radioactive peptide corresponding to the sequence Asn(39) Thr Gln Ala Thr Asn Arg Asn Thr Asp Gly Ser Thr Asp Tyr(53) in the enzyme. Digestion of this peptide with Clostridium histolyticum aminopeptidase gave a radioactive pentapeptide the composition, partial structure, and other properties of which corresponded to the sequence Gly(49) Ser Thr Asp Tyr(53) in hen egg white lysozyme, and which contained 2 moles of glucosamine per mole of peptide. The authors' findings show that the affinity label is covalently bound to the enzyme via the β carboxyl group of Asp 52 and are in accord with their conclusions from immunochemical and x ray crystallographic studies of the affinity labeled hen egg white lysozyme.
Note:
Related Files :
Amino Acids
Animal
chemistry
Chickens
egg white
Electrophoresis, Polyacrylamide Gel
Female
peptides
tritium
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
31169
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:00
Scientific Publication
Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme
248
Eshdat, Y., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
McKelvy, J.F., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
Sharon, N., Dept. Biophys., Weizmann Inst. Sci., Rehovoth, Israel
Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme
Hen egg white lysozyme, fully inactivated by the affinity labeling reagent, the 2',3' epoxypropyl β glycoside of di (N acetyl D glucosamine), contained 1 mole of the label per mole of protein. Total enzymatic digestion of the reduced and carboxymethylated affinity labeled enzyme afforded, as a major radioactive product, a compound composed solely of aspartic acid and glucosamine at the molar ratio of 1:2. Peptic digestion afforded a single radioactive peptide corresponding to the sequence Asn(39) Thr Gln Ala Thr Asn Arg Asn Thr Asp Gly Ser Thr Asp Tyr(53) in the enzyme. Digestion of this peptide with Clostridium histolyticum aminopeptidase gave a radioactive pentapeptide the composition, partial structure, and other properties of which corresponded to the sequence Gly(49) Ser Thr Asp Tyr(53) in hen egg white lysozyme, and which contained 2 moles of glucosamine per mole of peptide. The authors' findings show that the affinity label is covalently bound to the enzyme via the β carboxyl group of Asp 52 and are in accord with their conclusions from immunochemical and x ray crystallographic studies of the affinity labeled hen egg white lysozyme.
Scientific Publication
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