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Chemical Evidence For Identical Subunits In L-asparaginase From Escherichia Coli B.

A. Greenquist, J. C. Wriston
Published 1972 · Chemistry, Medicine

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Abstract Application of four independent methods for cystine indicate that there are eight half-cystines per mole of Escherichia coli B asparaginase, consistent with a four subunit model with one intrachain disulfide link per subunit. Treatment with dinitrofluorobenzene showed only leucine as NH 2 -terminal amino acid; values of 3.17–3.9 moles of DNP-Leu per mole of asparaginase were obtained. Hydrazinolysis released tyrosine as the principal amino acid, 3.3 residues per mole of protein being obtained. Studies with the carboxyl modification technique of Hoare and Koshland ( Hoare, D. G., and Koshland, D. E. (1967) J. Biol. Chem. 242, 2447 ) showed that 61% of the side chain carboxyl groups are present as amide. Studies with carboxypeptidase A demonstrated the carboxyl terminal sequence to be -(Ile, Glu, Asn)-Phe-Ile-Gln-Tyr. The results obtained by preparing two-dimensional peptide maps of the tryptic digest of reduced, S -aminoethylated enzyme are also in agreement with a four subunit model in which the subunits are identical or nearly so.
This paper references
Peptide separation by two-dimensional chromatography and electrophoresis.
A. Katz (1959)
10.1021/AC60206A024
Ion Exchange Chromatography of Amino Acids. A Single Column, High Resolving, Fully Automatic Procedure.
P. Hamilton (1963)
On the Aminoethylation of Proteins
Raftery Ma (1966)
10.1021/BI00855A011
Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity.
H. A. Campbell (1967)
10.1038/167767B0
Identification of N-2 : 4-Dinitrophenylamino-Acids
A. Lowther (1951)
10.1016/0005-2795(69)90191-3
Subunit structure of L-asparaginase from Escherichia coli B.
J. Kirschbaum (1969)
10.1016/S0076-6879(57)03420-5
[79] Identification of amino acids by paper chromatography
W. Stepka (1957)
10.1016/S0076-6879(67)11038-0
[36] Paper chromatography and electrophoresis; special procedure for peptide maps
J. Bennett (1967)
10.1128/JB.95.6.2117-2123.1968
New procedures for purification of L-asparaginase with high yield from Escherichia coli.
J. Roberts (1968)
On the determination of cystine as cysteic acid.
S. Moore (1963)
STUDIES ON THE CARBOXYL- AND AMINO-TERMINAL RESIDUES OF RABBIT MUSCLE ALDOLASE.
J. A. Winstead (1964)
The subunit structure of tryptophanase. II. A correlation of ultracentrifugal and chemical studies.
Y. Morino (1967)
10.1042/BJ0680475
The kinetics of hydrazinolysis of simple peptides in anhydrous hydrazine.
J. Bradbury (1958)
A method for the quantitative modification and estimation of carboxylic acid groups in proteins.
D. G. Hoare (1967)
10.1021/AC60139A006
Automatic recording apparatus for use in the chromatography of amino acids.
S. Moore (1958)
10.1016/0003-9861(68)90144-6
Primary structure of bovine carboxypeptidase B. II. Tryptic peptides from the reduced, aminoethylated protein.
M. Elzinga (1968)
10.1021/BI00837A042
L-Asparaginase EC-2 from Escherichia coli. Some substrate specificity characteristics.
H. A. Campbell (1969)
The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.
A. M. Crestfield (1963)
10.1016/S0076-6879(67)11050-1
[48] Leucine aminopeptidase (LAP)
A. Light (1967)
10.1016/0006-3002(54)90233-4
C-Terminal groups in myosin, tropomyosin and actin.
R. Locker (1954)
The complete enzymic hydrolysis of proteins.
R. L. Hill (1962)
Protein measurement with the Folin phenol reagent.
O. H. Lowry (1951)
Crystalline L-asparaginase from Escherichia coli B. II. Physical properties, subunits, and reconstitution behavior.
B. Frank (1970)
10.1016/0022-2836(69)90470-7
Molecular properties of acetylcholinesterase.
W. Leuzinger (1969)
The sequence of the amino acid residues in performic acid-oxidized ribonuclease.
C. Hirs (1960)
A reinvestigation of the sequence of residues 11 to 18 in bovine pancreatic ribonuclease.
J. Potts (1962)
Crystalline L-asparaginase from Escherichia coli B. I. Purification and chemical characterization.
P. Ho (1970)
10.1515/BCHM2.1970.351.1.197
Isolation and properties of L-asparaginases from Escherichia coli.
A. Arens (1970)
10.1021/BI00834A020
Purification and properties of asparaginase from escherichia coli B.
H. A. Whelan (1969)
10.1042/BJ0480126
The separation of N-2:4-dinitrophenly amino-acids on paper chromatograms.
S. Blackburn (1951)
10.5555/URI:PII:0022214356900646
A simple ultraviolet spectrophotometric method for the determination of protein.
W. Waddell (1956)
10.1016/0304-4165(65)90147-9
Combinations of specific color reactions useful in the peptide mapping technique.
C. Easley (1965)
10.1111/J.2164-0947.1968.TB02511.X
L-asparaginase: the evolution of a new tumor inhibitory agent.
J. Broome (1968)



This paper is referenced by
10.1007/BF00335825
Factors affecting l-asparaginase activity in soils
W. Frankenberger (2004)
Bioinformatic Analysis of L-Asparaginase II from Citrobacter Freundii 1101, Erwinia Chrysanthemi DSM 4610, E. coli BL21 and Klebsiella Pneumoniae ATCC 10031
K. Aghaiypour (2017)
10.1021/BI00748A010
Purification and partial sequencing of cyanogen bromide peptides from L-asparaginase of Escherichia coli B.
J. G. Gumprecht (1973)
Systematic site-directed mutagenesis to characterize subunit interactions in E. coli asparaginase II, an enzyme
S. Verma (2005)
10.1111/J.1432-1033.1996.0201T.X
Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase.
J. Lubkowski (1996)
10.1107/S0907444900020175
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
M. Jaskólski (2001)
10.1016/0005-2795(74)90266-9
Purification and properties of L-asparaginase from Serratia marcescens.
H. A. Whelan (1974)
10.1016/0014-5793(75)80726-5
Studies on conformation and antigenicity of reduced S‐methylated asparaginase in comparison with asparaginase
K. Todokoro (1975)
10.1080/10826068.2013.833116
AN OPTIMIZED PROTOCOL FOR OVERPRODUCTION OF RECOMBINANT PROTEIN EXPRESSION IN Escherichia coli
E. Bahreini (2014)
10.1016/0014-5793(76)80610-2
Modification of cystine or tryptophan residues in the asparaginase molecule and their role in conformation and antigenicity
T. Saito (1976)
10.1186/1556-276X-9-340
Preparation and nanoencapsulation of l-asparaginase II in chitosan-tripolyphosphate nanoparticles and in vitro release study
E. Bahreini (2014)
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