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Studies on plant amylases
Open accessAbstract
IT is clear that, for the determination of enzymic reaction-velocity under readily definable conditions, the states near the initiation of the reaction are decidedly the best.Usually however this part of the progress has been left unexplored and delineation of it has been based merely upon empirical expressions of doubtful value.In the present paper data have been directly collected within a few minutes of the origination of the reaction on the mixing of enzyme and sub- strate.From these data "initial slopes"' are determined graphically and used as a measure of reaction-velocity.In experiments of this short duration the difference between apparent and true zero-time becomes significant. THE STARCH-AMYLASE SYSTEMI. DESCRIPTION OF AN "INITIAL SLOPE MIETHOD.
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Cited by
Isolation of a Calcium-Sequestering Protein from Sarcoplasmic Reticulum
MacLennan, D. H., & Wong, P. T. S. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.6.1231 · Cited by 567
Staphyloferrin A: a structurally new siderophore from staphylococci
KONETSCHNY‐RAPP, S., JUNG, G., MEIWES, J., & ZÄHNER, H. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19094.x · Cited by 160
Metadata
- Authors
- Hanes, C. S.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1932-01-01
- Volume
- 26
- Issue
- 5
- Pages
- 1406-1421
- ISSN
- 0306-3283 (ISSN-L)
- OpenAlex
- W2409770357
- Cited by
- 735
- References
- 0
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Hanes, C. S. (1932). Studies on plant amylases. Biochemical Journal. https://doi.org/10.1042/bj0261406
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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