Isolation and in vitro translation of soybean leghaemoglobin mRNA View Full Text


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Article Info

DATE

1974-09

AUTHORS

DESH PAL S. VERMA, DUDLEY T. NASH, HERBERT M. SCHULMAN

ABSTRACT

LEGHAEMOGLOBIN (Lb), a myoglobin-like protein, is found in large quantities in the root nodules which result from the symbiotic association between the bacterium Rhizobium and plants of the family Leguminosae. The probable function of Lb is the regulation of intranodule oxygen tension1 and its presence is correlated with rhizobial nitrogenase2. The haem prosthetic group of Lb is of bacterial origin3 and the plant contains the genetic determinants for the apoprotein4,5. Soybean Lb consists of two major components of different electrophoretic mobility6. The faster component (LbF) is composed of 139 amino acids, has a molecular weight of 15,600 and contains an amino terminal glycine residue, while the slower component (LbS) is composed of 143 amino acids, has a molecular weight of 15,900 and contains an amino terminal valine residue. Because of these differences LbF and LbS are presumed to be different gene products7. Thus they are useful markers in studies on the transfer of plant genes involved in symbiosis to other plants. More... »

PAGES

74-77

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/251074a0

DOI

http://dx.doi.org/10.1038/251074a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048652287

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4414006


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