Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

Nature ◽  
1975 ◽  
Vol 255 (5510) ◽  
pp. 609-614 ◽  
Author(s):  
D. W. Banner ◽  
A. C. Bloomer ◽  
G. A. Petsko ◽  
D. C. Phillips ◽  
C. I. Pogson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Triose Phosphate Isomerase ◽  
Triose Phosphate ◽  
Amino Acid Sequence Data ◽  
Chicken Muscle

scholarly journals A monoclonal antibody that defines an idiotope with two subsites in galactan-binding myeloma proteins.

1981 ◽  
Vol 154 (6) ◽  
pp. 1946-1956 ◽  
Author(s):  
M Pawlita ◽  
E Mushinski ◽  
R J Feldmann ◽  
M Potter
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Molecular Models ◽  
Myeloma Protein ◽  
Amino Acid Sequence Data ◽  
Myeloma Proteins ◽  
Igg1 Monoclonal Antibody ◽  
Hybridoma Technology

An IgG1 monoclonal antibody HyX24-14 was derived from A/J mice that were immunized with the IgA XRPC24 (X24) galactan binding myeloma protein (GalBMP) of BALB/c origin by the Kohler-Milstein hybridoma technology. HyX24-14 specifically binds some but all GalBMP. Different patterns of binding using a panel of nine Gal BMP were found, depending upon the concentration of antibody and the antigenic target. From molecular models and amino acid sequence data, ti was proposed that the idiotope defined by HyX24-14 had two subsites, each of which appeared to be able to bind independently to the antibody.

Systematic relationships of the ranunculacea based on amino acid sequence data

1981 ◽  
Vol 20 (7) ◽  
pp. 1559-1565 ◽  
Author(s):  
Cornelia Grund ◽  
John Gilroy ◽  
Tim Gleaves ◽  
Uwe Jensen ◽  
Donald Boulter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Amino Acid Sequence Data ◽  
Systematic Relationships

Amino acid sequence data of α-tubulin from myxamoebae of Physarum polycephalum

1986 ◽  
Vol 192 (4) ◽  
pp. 919-924 ◽  
Author(s):  
Monika Singhofer-Wowra ◽  
Melvyn Little ◽  
Lesley Clayton ◽  
Peter Dawson ◽  
Keith Gull
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Physarum Polycephalum ◽  
Sequence Data ◽  
Amino Acid Sequence Data

scholarly journals Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle

1974 ◽  
Vol 139 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Anna J. Furth ◽  
J. D. Milman ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Rabbit Muscle ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Triose Phosphate

1. Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH4)2SO4 fraction of an extract of homogenized chicken breast muscle. The product is homogeneous on gel electrophoresis and is suitable for growing crystals for X-ray work. The specific activity is 10000 units/mg and the value for E0.1%280 is 1.20. 2. Comparison between the sum of the amino acid compositions of the tryptic peptides of the protein and the amino acid composition obtained on total hydrolysis of the protein indicates that the relative subunit mass is about 27000. 3. These data, together with the results of the examination of the amino acid compositions of a number of minor peptides, the number of peptides in the tryptic digest and the complete amino acid sequences of the tryptic peptides (the determination of which is described here), give no indication that the subunits are dissimilar. 4. A tentative amino acid sequence is presented for the protein, in which the ordering of the tryptic peptides is derived by homology with the sequence of the rabbit muscle enzyme (Corran & Waley, 1973). 5. An appendix describes the use that was made of mass spectrometry in the determination of some of the sequences. Mass-spectrometric data have been obtained for 35 residues, that is about 15% of the total sequence of the protein. 6. An extended version of the present paper has been deposited as Supplementary Publication SUP 50025 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

Sign in / Sign up

Export Citation Format

Share Document