Powered by OpenAIRE graph
Found an issue? Give us feedback
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Proceedings of the I...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Proceedings of the Indian Academy of Sciences - Section A Part 3 Mathematical sciences
Article . 1988 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
versions View all 1 versions
addClaim

Uptake and assimilation of nitrogen by marine diatoms—II. Kinetics of nitrogen assimilation

Authors: V Sivasubramanian; V N R Rao;

Uptake and assimilation of nitrogen by marine diatoms—II. Kinetics of nitrogen assimilation

Abstract

A comparison ofK M values for nitrate and nitrite reductases with uptake capacities of 6 marine diatoms indicated that intracellular accumulation of NO 3 − and NO 2 − is necessary for efficient functioning of the enzymes.Amphora coffeaeformis, Thalassiosira weissflogii andSynedra tabulata accumulated very little NO 3 − whereasTriceratium dubium, Achnanthes hauckiana andFragilaria pinnata accumulated 0·02 to 1· 5mM NO 2 − . Studies with inhibitors of nitrate and nitrite reductase indicated that nitrite reductase could be located i in a different compartment such as chromatophores as in higher plants. NH 4 + was also accumulated by the diatoms. Studies on the kinetics of glutamine synthetase and glutamate dehydrogenase indicated that the primary enzyme involved in NH 4 + assimilation could be glutamate dehydrogenase, because of its lowK 4 + and relatively greater activity than glutamine synthetase. Intracellular analysis of NH 4 + revealed that its concentration was well below theK 4 + for glutamine synthetase.

Related Organizations
  • BIP!
    Impact byBIP!
    selected citations
    These citations are derived from selected sources.
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    0
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Average
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Average
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Average
Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
Average
Average
Upload OA version
Are you the author of this publication? Upload your Open Access version to Zenodo!
It’s fast and easy, just two clicks!