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Studies on Adenosine Triphosphate Transphosphorylases
Open accessAbstract
1 This value refers to the acid molybdate-labile phosphate determination calculated according to the previous definition of the unit (1).More accurate determinations of the initial velocity by means of a recording pH-stat method (5) yield approximately 240 peq per mg of protein per minute for the specific activity under the conditions to be described.
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Citations
Cited by
A new acid hydrolysis method for determining tryptophan in peptides and proteins
Penke, B., Ferenczi, R., & Kovács, K. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90129-8 · Cited by 608
Hydrolysis and amino acid composition analysis of proteins
Fountoulakis, M., & Lahm, H.-W. (1998) · Journal of Chromatography A · doi:10.1016/s0021-9673(98)00721-3 · Cited by 606
Hill, R. L. (1965) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60388-5 · Cited by 411
Metadata
- Authors
- Noltmann, E. A., Mahowald, T. A., & Kuby, S. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1962-04
- Volume
- 237
- Issue
- 4
- Pages
- 1146-1154
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1574291960
- Cited by
- 204
- References
- 0
- FWCI
- 7.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Studies on Adenosine Triphosphate Transphosphorylases. https://app.cochat.ai/papers/10.1016/s0021-9258(18)60297-2
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- Noltmann, E. A., Mahowald, T. A., & Kuby, S. A. (1962). Studies on Adenosine Triphosphate Transphosphorylases. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)60297-2
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
