| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/0022-5193(78)90229-1 |
| P953 | full work available at URL | https://api.elsevier.com/content/article/PII:0022519378902291?httpAccept=text/plain |
| https://api.elsevier.com/content/article/PII:0022519378902291?httpAccept=text/xml | ||
| P698 | PubMed publication ID | 34067 |
| P2093 | author name string | C. Bauer | |
| U. Mura | |||
| P2860 | cites work | Estimation of the dissociation constants of enzyme-substrate complexes from steady-state measurements. Interpretation of pH-independence of Km | Q39096204 |
| PH-dependence of the steady-state rate of a two-step enzymic reaction | Q39102011 | ||
| Some kinetic aspects of the mechanism of hydrolysis of phosphoric acid esters by nonspecific acid phosphatase from Schizosaccharomyces pombe | Q39178324 | ||
| The effect of pH on the affinities of enzymes for substrates and inhibitors | Q39219141 | ||
| The effects of hydrogen ion concentration on the simplest steady-state enzyme systems | Q42114538 | ||
| Studies on sulphatase. II. The purification and properties of the arylsulphatase of Alcaligenes metalcaligenes | Q42145544 | ||
| Some aspects of the kinetics of enzymic reactions | Q73121942 | ||
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | modeling and simulation | Q6888384 |
| applied mathematics | Q33521 | ||
| chemical model | Q25109595 | ||
| P1104 | number of pages | 8 | |
| P304 | page(s) | 181-188 | |
| P577 | publication date | 1978-11-01 | |
| 1978-11-21 | |||
| P1433 | published in | Journal of Theoretical Biology | Q2153724 |
| P1476 | title | pH influence on enzymic activity: the involvement of two active ionized forms of either substrate or enzyme in the reaction | |
| PH influence on enzymic activity: The involvement of two active ionized forms of either substrate or enzyme in the reaction | |||
| P478 | volume | 75 |
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