NDLI: SPECIFICITY OF RECOMBINATION OF H AND L CHAINS FROM HUMAN γG-MYELOMA PROTEINS

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SPECIFICITY OF RECOMBINATION OF H AND L CHAINS FROM HUMAN γG-MYELOMA PROTEINS

Content Provider	Scilit
Author	Grey, Howard M. Mannik, Mart
Copyright Year	1965
Description	Journal: The Journal of experimental medicine Dissociated H and L chains of human γG-myeloma proteins were recombined by removal of conditions interrupting non-covalent interactions. In the process of recombination 7S molecules were formed. It was demonstrated that the H chains from individual γG-myeloma proteins recombine with their own L chains but also with L chains derived from other myeloma proteins. In some instances, however, the L chains from other myeloma proteins did not recombine as avidly with the H chains as the autologous L chains. The specificity of the non-covalent interactions of H and L chains was particularly well brought out by competitive recombination experiments where an individual H chain had a choice of recombining with its own L chain or with the L chain obtained from another myeloma protein. In this manner a spectrum of affinities between individual H chains and several L chains was demonstrated. In the vast majority of recombinations there was a clearcut preference for recombination to take place between the H and L chains derived from the same protein. It is postulated that this specificity is related to differences in the primary structure, which cause differences in configuration of these homogeneous H and L chains and that these configurations then dictate on thermodynamic grounds the pairing of H chains with particular L chains.
Related Links	http://jem.rupress.org/content/122/3/619.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138072/pdf
ISSN	00221295
DOI	10.1084/jem.122.3.619
Journal	The Journal of experimental medicine
Issue Number	3
Volume Number	122
Language	English
Publisher	Rockefeller University Press
Publisher Date	1965-09-01
Access Restriction	Open
Subject Keyword	Journal: The Journal of experimental medicine Physical Chemistry Ultracentrifugation Gamma Globulins
Content Type	Text
Resource Type	Article
Subject	Physiology

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