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Institut National De La Sante Et De La Recherche Medicale

Virginia Commonwealth University

Meristern Therapeutics

Claude Poyart

Veronique Gruber

Bertrand Merot

Philippe Lenee

Sylvie Baudino

Michael Marden

Wilfrid Dieryck

Renee-Josee Pagnier

Donald J Abraham

A method for producing haemin proteins by (i) inserting into plant cells one or more nucleic acid molecules that each comprise at least one sequence coding for a protein component of an animal haemin protein capable of reversibly binding oxygen, or for a variant or portion of said protein component, and optionally a sequence coding for a selection agent; (ii) selecting cells containing nucleic acid coding for the protein component of the haemin protein; (iii) optionally propagating the transformed cells either in a culture or by regenerating whole transgenic or chimeric plants; and (iv) recovering and optionally purifying a haemin protein that includes a complex consisting of the protein or proteins coded for by said nucleic acid and at least one iron-containing porphyritic nucleus, or a plurality of such complexes.

Method for producing hemin proteins using plant cells, resulting proteins and products containing same

A method for producing human hemoglobin proteins by (i) inserting into plant cells one or more nucleic acid molecules that each comprise at least one sequence coding for a protein component of a human hemoglobin protein capable of reversibly binding oxygen, and optionally a sequence coding for a selection agent; (ii) selecting cells containing nucleic acid coding for the protein component of the human hemoglobin protein; (iii) optionally propagating the transformed cells either in a culture or by regenerating whole transgenic or chimeric plants; and (iv) recovering and optionally purifying the human hemoglobin protein that includes a complex consisting of the protein or proteins coded for by the nucleic acid and at least one iron-containing polphyritic nucleus, or a plurality of such complexes.

Method for producing human hemoglobin proteins using plant cells

Drug compounds are used as allosteric modifiers of hemoglobin present in red blood cells. The compounds bind to only a single pair of symmetry related sites in the central water cavity of hemoglobin at the Lys 99.alpha., Arg 141.alpha., and Asn 108 .beta. residues. When one of the drug compounds is bound to hemoglobin, it will join three separate sub-units of the hemoglobin molecule and stabilize the hemoglobin in a lower oxygen affinity state. Because the compounds used in this method are either not bound by serum albumin or only interact to small degrees with serum albumin, the compounds are active in whole blood and in vivo. The process of allosterically modifying hemoglobin towards a low oxygen affinity state in whole blood and in vivo could be used in a wide variety of applications including in treatments for ischemia, heart disease, wound healing, Alzheimer's, depression, schizophrenia, adult respiratory distress syndrome (ARDS), etc., in extending the shelf-life of blood or restoring the oxygen carrying capacity of out-dated blood, and as sensitizers for x-ray irradiation in cancer therapy, as well as in many other applications.

Method for lowering oxygen affinity of hemoglobin in redcell

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Paris, France

Claude Poyart