| Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms. Jabusch J.R., Bray R.P., Deutsch H.F.
J. Biol. Chem. 255:9196-9204(1980) · UniProtKB (1) |
| Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase. Jabusch J.R., Farb D.L., Kerschensteiner D.A., Deutsch H.F.
Biochemistry 19:2310-2316(1980) · UniProtKB (1) |
| Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. Lin K.-T.D., Deutsch H.F.
J. Biol. Chem. 248:1885-1893(1973) · UniProtKB (1) |
| Primary structure of the Mcg lambda chain. Fett J.W., Deutsch H.F.
Biochemistry 13:4102-4114(1974) · UniProtKB (2) |
| Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. Lin K.-T.D., Deutsch H.F.
J. Biol. Chem. 249:2329-2337(1974) · UniProtKB (2) |
| The sequence of equine muscle carbonic anhydrase. Wendorff K.M., Nishita T., Jabusch J.R., Deutsch H.F.
J. Biol. Chem. 260:6129-6132(1985) · UniProtKB (1) |
| Analyses of polypeptides in the liver of a novel mutant (LEC rats) to hereditary hepatitis and hepatoma by two-dimensional gel electrophoresis: identification of P29/6.8 as carbonic anhydrase III and triosephosphate isomerase. Nagase T., Sugiyama T., Kawata S., Tarui S., Deutsch H.F., Taniguchi N.
Comp. Biochem. Physiol. 99B:193-201(1991) · UniProtKB (1) |
| A new lambda-chain gene. Fett J.W., Deutsch H.F.
Immunochemistry 12:643-652(1975) · UniProtKB (1) |
