William Marsh Rice University

Other

Wisconsin Alumni Research Foundation

The Children's Hospital of Philadelphia

Baxter Biotech Technology Sarl

Baxter Biotech Technology Saarl

John S Olson

Antony James Mathews

Daniel H Doherty

Christopher B Glascock

Douglas D Lemon

Michael J Weickert

Kyoshi Nagai

Jacqueline F Aitken

Mark S Hargrove

Timothy L Whitaker

George N Phillips, Jr

Mitchell Weiss

Janet Braam

Katsiaryna Hleb

Dmitri Lapotko

Methods, systems, and apparatuses for employing nanobubbles for theranostic purposes are provided. In one embodiment, a method comprising introducing a photothermal nanobubble into a malaria-infected red blood cell is provided.

Theranostic methods and systems for diagnosis and treatment of malaria

The disclosure relates to recombinant adult human apohemoglobin (apo-rHb) in which the stability has been increased by replacement of an amino acid with a counterpart from another organism, such as a deep sea diving mammal. This mutated apo-rHb may be more stable and/or give higher production yields than unmutated adult human apo-rHb. The mutated apo-rHb may be produced in microorganisms, such asor yeast cells, or animal erythroid cells. Some apo-rHb of the present disclosure may be used as part of a blood substitute.

Increasing the stability of recombinant adult human apohemoglobin

The present disclosure relates to the use of AHSP to stabilize the &#x3b1; subunit of rHb. AHSP may be co-expressed with the hemoglobin genes. AHSP stabilization may be used to increase the production of intact rHb in various systems, such as, other microorganisms, or animal erythroid cells. This intact rHb may then be used as part of a blood substitute product.

Enhancing recombinant hemoglobin production by co-expression with alpha hemoglobin stabilizing protein

The invention relates to novel recombinant hemoglobins having reduced nitric oxide scavenging and/or increased high soluble expression. The invention further relates to methods of increasing the soluble expression of recombinant hemoglobin by adding exogenous hemin in molar excess of the heme binding sites of recombinant hemoglobin.

Hemoglobin mutants with increased soluble expression and/or reduced nitric oxide scavenging

The present invention relates to methods of reducing heme loss in hemoglobins to produce stability and improve expression yield of hemoglobins, particularly recombinant hemoglobins. Such methods are accomplished by introducing mutations in the alpha or beta subunits of hemoglobins to increase heme affinity. The present invention further relates to novel mutations that reduce such heme loss.

Hemoglobin mutants that reduce heme loss

This invention relates to recombinant hemoglobins containing mutations in or near the heme pocket of the hemoglobin molecule. This invention particularly relates to recombinant hemoglobins that have altered geometry or polarity around the distal portion of the heme pocket.

Nucleic acids encoding mutant recombinant hemoglobins containing heme pocket mutations

Mutant recombinant hemoglobins containing heme pocket mutations

Growing community of inventors

Houston, TX, United States of America

John S Olson