[go: up one dir, main page]

Rose, 1969 - Google Patents

Evidence for histidine in the triethyltin-binding site of rat haemoglobin

Rose, 1969

View PDF
Document ID
11349433276849273693
Author
Rose M
Publication year
Publication venue
Biochemical Journal

External Links

Snippet

One molecule of rat haemoglobin binds two molecules of triethyltin. The binding sites are located on the globin and there is co-operativity between the sites such that the intrinsic affinity constant at pH8· 0 increases from 3· 5× 105m− 1 for the binding of the first triethyltin …
Continue reading at pmc.ncbi.nlm.nih.gov (PDF) (other versions)

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/745—Blood coagulation or fibrinolysis factors

Similar Documents

Publication Publication Date Title
Rose Evidence for histidine in the triethyltin-binding site of rat haemoglobin
Partridge et al. The chemistry of connective tissues. 3. Composition of the soluble proteins derived from elastin
McMENAMY et al. Unbound amino acid concentrations in human blood plasmas
Andersson The heterogeneity of bovine serum albumin
Dus et al. Chemical characterization of high potential iron proteins from Chromatium and Rhodopseudomonas gelatinosa
Haour et al. Characterization and solubilization of gonadotropin receptor of bovine corpus luteum
Deuticke et al. Stereoselective, SH-dependent transfer of lactate in mammalian erythrocytes
Harfenist et al. The molecular weight of insulin
Nowak et al. Agglutinin from Limulus polyphemus: purification with formalinized horse erythrocytes as the affinity adsorbent
Johnson et al. Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate
Zinneman et al. On the nature of cryoglobulins
Kosower et al. Dynamic changes of red cell membrane thiol groups followed by bimane fluorescent labeling
Fahey et al. Analysis of biological thiols: derivatization with monobromotrimethylammoniobimane and characterization by electrophoresis and chromatography
Thomas et al. Partial characterization of a low-molecular weight methylmercury complex in rat cerebrum
Ruiz-Carrillo et al. A method for the purification of histone fraction F3 by affinity chromatography
Evans et al. Bovine Erythrocyte Superoxide dismutase: Isolation and characterization of tryptic, cyanogen bromide, and maleylated tryptic peptides
IE53534B1 (en) Process and reagent for the determination of glycosilated haemoglobin
Beaven et al. Binding of protoporphyrin and haemin to human spectrin
Cohen Glycosaminoglycans are integral constituents of renal glomerular basement membrane
Cassoly Interaction of hemoglobin with the red blood cell membrane. A saturation transfer electron paramagnetic resonance study
Corthésy et al. The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance
Brown et al. Reaction of reactive sulfhydryl groups of creatine kinase with dansyl chloride
Terwilliger et al. Molecular weight of Eudistylia vancouveri chlorocruorin and its subunits
Harris et al. The carboxymethylation of human metmyoglobin
Hunneyball et al. Subfragmentation of the Fc fragment of human IgG1 myeloma protein by thermolysin