Immunological Detection of Single Amino Acid Substitutions in Alkaline Phosphatase
- 11 April 1969
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 164 (3876), 188-189
- https://doi.org/10.1126/science.164.3876.188
Abstract
Antiserums to wild-type alkaline phosphatase from Escherichia coli were prepared and tested for reactivity with phosphatases altered by point mutations. Eight out of the nine mutant enzymes were distinguished from the wild type with quantitative microcomplement fixation. The structural changes are among the smallest yet observed immunologically.Keywords
This publication has 24 references indexed in Scilit:
- Amino acid sequence of T2 phage lysozymeJournal of Molecular Biology, 1968
- Molecular Size of Hagfish Muscle Lactate DehydrogenaseScience, 1967
- The coat protein of the RNA bacteriophage MS2Journal of Molecular Biology, 1967
- Base composition of nonsense codons in Escherichia coli: The N2 codon UAAJournal of Molecular Biology, 1967
- Quantitative Immunochemistry and the Evolution of Primate Albumins: Micro-Complement FixationScience, 1966
- The properties and interactions of the isolated α- and β-chains of human haemoglobinJournal of Molecular Biology, 1966
- Antibodies to human A1 hemoglobin and their reaction with A2, S, C, and H hemoglobinsImmunochemistry, 1964
- Hybrid protein formation of E. coli alkaline phosphatase leading to in vitro complementationJournal of Molecular Biology, 1963
- Fingerprint analysis of alkaline phosphatase of Escherichia coli K12Journal of Molecular Biology, 1963
- A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphataseBiochimica et Biophysica Acta, 1960