40 results about "Hemoglobin F" patented technology

A method of determining glycated hemoglobin is provided, by which a ratio of the glycated hemoglobin in a sample can be determined accurately and easily. The ratio of glycated hemoglobin can be determined by degrading a glycated hemoglobin in a whole blood sample selectively with a protease to give a glycated hemoglobin degradation product; causing a redox reaction between a glycation site of the glycated hemoglobin degradation product and a fructosyl amino acid oxidoreductase; and determining this redox reaction. Further, as shown in FIG. 1, in a whole blood sample, there is a correlation between the ratio of the glycated hemoglobin determined by this method and an HbA1c concentration. Thus, without determining the glycated α-amino group as a characteristic structure of HbA1c, an amount of HbA1c can be determined accurately and easily from the determined ratio of the glycated hemoglobin.

The present invention relates to novel methods of using blood substitutes to treat acute blood loss and novel pharmaceutical compositions comprising blood substitutes. Blood substitutes useful for the methods of the present invention can (1) induce expression of erythropoietin as tested in a cell culture under normoxic conditions, and / or (2) induce erythropoiesis under normoxic conditions as measured by (a) a decrease in the doubling time of the subject's hematocrit or hemoglobin, and / or (b) an increase in the subject's circulating erythropoietin level. Blood substitutes useful for the pharmaceutical compositions of the present invention can (1) stabilize HIF-1 alpha expression, and / or (2) down regulate NF-kappa B. Preferably, the blood substitutes are cross-linked hemoglobin blood substitutes, or more preferably, cross-linked hemoglobins that comprise a hemoglobin that is cross-linked intramolecularly with periodate-oxidized ATP, cross-linked intermolecularly with periodate-oxidized adenosine, and conugated with reduced glutathione.

A method for improving the oxygen-releasing ability of hemoglobin, hemoglobin variants, recombinant hemoglobin and hemoglobin-based blood substitutes to organs and peripheral tissues in human bodies is disclosed by administering a compound of phthalides to a subject in need thereof to improve the oxygen-releasing ability of hemoglobin, hemoglobin variants, recombinant hemoglobin and hemoglobin-based blood substitutes to the organs and the peripheral tissues in human bodies. The compound of phthalides is characterized by a phthalide functional group, and forms at least one hydrogen bond with [alpha]Arg141 of hemoglobin, hemoglobin variants, recombinant hemoglobin and hemoglobin-based blood substitutes, stabilizing the [alpha]1 / [alpha]2 interface of hemoglobin, further stabilizing the oxygenated hemoglobin, hemoglobin variants, recombinant hemoglobin and hemoglobin-based blood substitutes in the low oxygen affinity 'T' state and facilitating the oxygen release to the organs and the peripheral tissues. A medication for improving the oxygen-releasing ability of hemoglobin, hemoglobin variants, recombinant hemoglobin, and hemoglobin-based blood substitutes to organs and peripheral tissues in human bodies is also disclosed.

Construct-complexes of a hemoglobin, a hepatocyte modifying substance bound to the hemoglobin, and a haptoglobin bound to the hemoglobin, are provided, for administration to mammalian patients. The construct-complex may be formed ex vivo, or a hemoglobin-hepatocyte modifying substance combination may be administered to the patient so that haptoglobin in the mammalian body bonds thereto to form the construct-complex in vivo. Disorders of the liver may be diagnosed and treated using construct-complexes described herein.

An hemoglobin (Hb)-Dextran (Dx) conjugate having a molecular weight between 50 kd and 500 kD provides a blood substitute that results in acceptable erythrocyte sedimentation rate (ESR) and excretion rate (EXC) values. DxHb conjugates of the invention can be used for a variety of purposes as an alternative to blood.

Provided herein are methods for detecting glycated hemoglobin in, for example, human whole blood, that are not affected by the presence of variation in amino acid sequence that can exist in hemoglobin β chains. The methods detect all glycated hemoglobin in a sample, regardless of the form of the hemoglobin that has been glycated, and thus detect glycated human Hemoglobin A, Hemoglobin S, and Hemoglobin C.

The invention belongs to the technical field of biomedical engineering, and is characterized in that: the sensor is composed of two photoelectric receiving tubes and at least three light sources with different light-emitting wavelengths, based on the different spectral characteristics of oxygenated and reduced hemoglobin and tissue background in tissue oxygen metabolism, According to the law of light absorption and scattering in tissues, the concentration of oxygenated and reduced hemoglobin in local tissues is calculated. The light sources with at least three wavelengths and the two photoelectric receiving tubes are arranged in a straight line at a certain distance, and the light sources can respectively emit red light and near-infrared light. It can sensitively detect the absolute amount of oxygenated and reduced hemoglobin in human tissue.

The invention discloses a nucleic acid aptamer of glycosylated hemoglobin GHb with high specificity and high affinity and a preparation method thereof. The nucleotide sequence of the glycosylated hemoglobin GHb nucleic acid aptamer includes any one of SEQ ID NO: 1 to SEQ ID NO: 4. The nucleic acid aptamer preparation method of glycosylated hemoglobin GHb includes: construction of random sequence oligonucleotide library, preparation of glycosylated hemoglobin-micromagnetic bead complex, initial screening of target substance-nucleic acid complex, and preparation of secondary single-stranded DNA oligonucleotide library , Screening and identification of glycosylated hemoglobin nucleic acid aptamers. The prepared nucleic acid aptamer is non-toxic, has a small molecular weight, is easy to synthesize and label, only specifically recognizes glycosylated hemoglobin GHb, does not recognize and bind to other homologous non-glycosylated hemoglobin Hb, and can become a molecular beacon for detecting the content of glycosylated hemoglobin GHb.

The present invention relates to the synthesis of functional human hemoglobin and other proteins in erythroid tissues of transgenic non-human animals and erythroid cell lines. It is based on the discovery that two of the five hypersensitivity sites of the beta-globin locus are sufficient to result in high level expression of human alpha- or beta-globin transgenes.