Gertrúd Szabolcsi
Affiliations: | Biological Research Centre | Hungarian Academy of Sciences, Budapest, Hungary |
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| Cseke E, Szabolcsi G. (1983) Enzyme-enzyme interactions within human erythrocytes as suggested from prelytic release. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 18: 151-61 |
| Solti M, Biszku E, Sajgó M, et al. (1975) Some structural features of rabbit muscle aldolase as derived from its limited proteolysis. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 10: 185-99 |
| Földi J, Szabolcsi G, Friedrich P. (1973) Interaction of glycolytic enzymes: increase of the apparent molecular weight of aldolase in rabbit muscle extract. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 8: 263-5 |
| Závodszky P, Biszku E, Abaturov LV, et al. (1972) Effect of thiol blocking and substrate binding on the conformation and conformational stability of rabbit muscle aldolase. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 7: 1-10 |
| Szajáni B, Sajgó M, Biszku E, et al. (1970) Identification of a cysteinyl residue involved in the activity of rabbit muscle aldolase. European Journal of Biochemistry / Febs. 15: 171-8 |
| Szajáni B, Friedrich P, Szabolcsi G. (1969) Inhibition of rabbit skeletal muscle aldolase by an alkylating agent. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 4: 265-72 |
| FRIEDRICH P, POLGAR L, SZABOLCSI G. (1964) THE EXISTENCE OF A HISTIDINE RESIDUE ESSENTIAL FOR GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ACTION. Acta Physiologica Academiae Scientiarum Hungaricae. 25: 217-28 |
| SZABOLCSI G, BOROSS L, BISZKU E. (1964) SECONDARY REACTIONS FOLLOWING BLOCKING OF ENZYME SH GROUPS. Acta Physiologica Academiae Scientiarum Hungaricae. 25: 149-59 |
| Friedrich P, Polgár L, Szabolcsi G. (1964) Effect of photo-oxidation on glyceraldehyde-3-phosphate Dehydrogenase Nature. 202: 1214-1215 |
| SZABOLCSI G, BISZKU E, SZORENYI E. (1959) Comparative studies on D-glyceraldehyde-3-phosphate dehydrogenase. VII. Studies on the digestibility of the enzyme isolated from various mammals. Biochimica Et Biophysica Acta. 35: 237-41 |