Patents
Literature
Hiro is an intelligent assistant for R&D personnel, combined with Patent DNA, to facilitate innovative research.
Hiro

122 results about "Hemeprotein" patented technology

A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.

Nonsymbiotic plant hemoglobins to maintain cell energy status

Nonsymbiotic hemoglobins are broadly present across evolution; however, the function of these proteins is unknown. Cultured maize cells have been transformed to constitutively express a barley hemoglobin gene in either the sense (HB+) or antisense (HB−) orientation. Hemoglobin protein in the transformed cell lines was correspondingly higher or lower than in wild type cells under normal atmospheric conditions. Limiting oxygen availability, by placing the cells in a nitrogen atmosphere for 12 hours, had little effect on the energy status of cells constitutively expressing hemoglobin, but had a pronounced effect on both wild type and HB− cells, where ATP levels declined by 27% and 61% respectively. Energy charge was relatively unaffected by the treatment in HB+ and wild type cells, but was reduced from 0.91 to 0.73 in HB− cells suggesting that the latter were incapable of maintaining their energy status under the low oxygen regime. Similar results were observed with P. aeruginosa cells transformed with an Hb expression vector. It is suggested that nonsymbiotic hemoglobins act to maintain the energy status of cells in low oxygen environments and that they accomplish this effect by promoting glycolytic flux through NADH oxidation, resulting in increased substrate level phosphorylation. Nonsymbiotic hemoglobins are likely ancestors of an early form of hemoglobin that sequestered oxygen in low oxygen environments, providing a source of oxygen to oxidize NADH to provide ATP for cell growth and development. This in turn suggests that cells containing increased levels of Hb protein will survive longer under low oxygen tension or high energy demand.
Owner:UNIVERSITY OF MANITOBA

Method for detecting concentration of ferrohemoglobin by using fluorescent carbon dot probe

The invention discloses a method for detecting the concentration of ferrohemoglobin by using a fluorescent carbon dot probe. The method comprises the following steps: 1, preparing different concentrations of fluorescent carbon dot-containing ferrohemoglobin standard solutions, detecting the fluorescence intensity of the standard solutions to obtain a standard solution fluorescence spectrogram, and establishing a linear relation between a difference between the fluorescence intensity of the standard solution with the ferrohemoglobin concentration being 0 and the fluorescence intensity of every standard solution and the ferrohemoglobin concentrations; and 2, preparing a fluorescent carbon dot-containing ferrohemoglobin sample solution, detecting the fluorescence intensity of the sample solution, and determining the concentration of ferrohemoglobin in the sample solution through the linear relation. The ferrohemoglobin concentration is detected by using the characteristics of a ferrohemoglobin quenching fluorescence carbon dot with the fluorescence carbon dot as a probe, so the method has the advantages of simple and convenient detection process, high sensitivity and low detection limit, and can realize online, in-situ, rapid and sensitive detection of the concentration of ferrohemoglobin in a practical sample.
Owner:GUANGXI TEACHERS EDUCATION UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products