Differential Binding Properties of Cytochrome c: Possible Relevance for Mitochondrial Ion Transport

Nature ◽  
1970 ◽  
Vol 228 (5273) ◽  
pp. 723-726 ◽  
Author(s):  
E. MARGOLIASH ◽  
G. H. BARLOW ◽  
V. BYERS
Keyword(s):  
Cytochrome C ◽  
Ion Transport ◽  
Binding Properties ◽  
Differential Binding

Differential binding properties of some opiates and opioid peptides

1979 ◽  
pp. 366-374 ◽  
Author(s):  
Ian Creese ◽  
Steven R. Childers ◽  
Rabi Simantov ◽  
Solomon H. Snyder
Keyword(s):  
Opioid Peptides ◽  
Binding Properties ◽  
Differential Binding

Antibodies Against B7-DC with Differential Binding Properties Exert Opposite Effects

Hybridoma ◽  
2012 ◽  
Vol 31 (1) ◽  
pp. 40-47 ◽  
Author(s):  
Patcharee Ritprajak ◽  
Masaaki Hashiguchi ◽  
Hisaya Akiba ◽  
Hideo Yagita ◽  
Ko Okumura ◽  
...  
Keyword(s):  
Binding Properties ◽  
Differential Binding

3.P.365 Differential binding properties of platelet derived growth factor isoforms to glycosaminoglycans

1997 ◽  
Vol 134 (1-2) ◽  
pp. 275
Author(s):  
F. Lustig ◽  
J. Hoebeke ◽  
C. Simonson ◽  
G. Östergren-Lundén ◽  
G. Fager
Keyword(s):  
Growth Factor ◽  
Platelet Derived Growth Factor ◽  
Binding Properties ◽  
Differential Binding

Differential binding properties of protein A and protein G for dog immunoglobulins

1991 ◽  
Vol 145 (1-2) ◽  
pp. 255-258 ◽  
Author(s):  
Zhikang Peng ◽  
F. Estelle ◽  
R. Simons ◽  
Allan B. Becker
Keyword(s):  
Protein A ◽  
Protein G ◽  
Binding Properties ◽  
Differential Binding

Differential binding properties of oripavines at cloned μ- and δ-opioid receptors

1999 ◽  
Vol 378 (3) ◽  
pp. 323-330 ◽  
Author(s):  
Katherine O Lee ◽  
Huda Akil ◽  
James H Woods ◽  
John R Traynor
Keyword(s):  
Opioid Receptors ◽  
Binding Properties ◽  
Differential Binding

scholarly journals Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)

2002 ◽  
Vol 367 (3) ◽  
pp. 653-664 ◽  
Author(s):  
Albert M. WU ◽  
June H. WU ◽  
Ming-Sung TSAI ◽  
Jia-Hau LIU ◽  
Sabine ANDRÉ ◽  
...  
Keyword(s):  
Blood Group ◽  
Lectin Binding ◽  
Binding Properties ◽  
Lectin Domain ◽  
Cell Matrix ◽  
Endogenous Lectins ◽  
Differential Binding ◽  
Definition Of ◽  
Domain I ◽  
Blood Group Abh

Galectins, a family of β-galactoside-specific endogenous lectins, are involved in regulating diverse activities such as proliferation/apoptosis, cell—cell (matrix) interaction and cell migration. It is presently unclear to what extent the carbohydrate fine specificities of the combining sites of mammalian galectins overlap. To address this issue, we performed an analysis of the carbohydrate-recognition domain (CRD-I) near the N-terminus of recombinant rat galectin-4 (G4-N) by the biotin/avidin-mediated microtitre plate lectin-binding assay with natural glycoproteins (gps)/polysaccharide and by the inhibition of galectin—glycan interactions with a panel of glycosubstances. Among the 35 glycans tested for lectin binding, G4-N reacted best with human blood group ABH precursor gps, and asialo porcine salivary gps, which contain high densities of the blood group Ii determinants Galβ1-3GalNAc (the mucin-type sugar sequence on the human erythrocyte membrane) and/or GalNAcα1-Ser/Thr (Tn), whereas this lectin domain reacted weakly or not at all with most sialylated gps. Among the oligosaccharides tested by the inhibition assay, Galβ1-3GlcNAcβ1-3Galβ1-4Glc was the best. It was 666.7 and 33.3 times more potent than Gal and Galβ1-3GlcNAc, respectively. G4-N has a preference for the β-anomer of Gal at the non-reducing ends of oligosaccharides with a Galβ1-3 linkage, over Galβ1-4 and Galβ1-6. The fraction of Tn glycopeptide from asialo ovine submandibular glycoprotein was 8.3 times more active than Galβ1-3GlcNAc. The overall carbohydrate specificity of G4-N can be defined as Galβ1-3GlcNAcβ1-3Galβ1-4Glc (lacto-N-tetraose)>Galβ1-4GlcNAcβ1-3Galβ1-4Glc (lacto-N-neo-tetraose) and Tn clusters>Galβ1-4Glc and GalNAcβ1-3Gal>Galβ1-3GalNAc>Galβ1-3GlcNAc>Galβ1-4GlcNAc>GalNAc>Gal. The definition of this binding profile provides the basis to detect differential binding properties relative to the other galectins with ensuing implications for functional analysis.

scholarly journals A Naturally Occurring Mutation in FcγRIIA: A Q to K127 Change Confers Unique IgG Binding Properties to the R131 Allelic Form of the Receptor

Blood ◽  
1998 ◽  
Vol 91 (2) ◽  
pp. 656-662 ◽  
Author(s):  
Cynthia F. Norris ◽  
Luminita Pricop ◽  
Sean S. Millard ◽  
Scott M. Taylor ◽  
Saul Surrey ◽  
...  
Keyword(s):  
Disease Susceptibility ◽  
Screening Methods ◽  
Allelic Form ◽  
Fcγ Receptors ◽  
Binding Properties ◽  
Naturally Occurring ◽  
Igg Binding ◽  
Polymorphic Forms ◽  
Differential Binding ◽  
Therapeutic Monoclonal Antibodies

Abstract FcγRIIa is widely expressed on hematopoietic cells. There are two known allelic polymorphic forms of FcγRIIa, FcγRIIa-R131 and FcγRIIa-H131, which differ in the amino acid at position 131 in the second Ig-like domain. In contrast to FcγRIIa-R131, FcγRIIa-H131binds hIgG2 but not mIgG1, and this differential binding has clinical implications for host defense, autoimmune disease, immunohematologic disease, and response to therapeutic monoclonal antibodies. We identified a novel FcγRIIA genotype in a healthy individual homozygous for FcγRIIA R/R131 in whom a C to A substitution at codon 127 changes glutamine (Q) to lysine (K) in one of the two FcγRIIA genes. This individual's homozygosity for FcγRIIA-R/R131 leads to the prediction that the receptors on her cells would not bind hIgG2. Monocyte and neutrophil phagocytosis of hIgG2-opsonized erythrocytes was significantly higher (P < .05) for cells from this K/Q127, R/R131 individual than for Q/Q127, R/R131 donors. Platelet aggregation stimulated by an mIgG1 anti-CD9 antibody in this individual was significantly different (P < .05) from Q/Q127, H/R131 and Q/Q127, H/H131 donors and similar to Q/Q127, R/R131. Our data show that the K127/R131 receptors have a unique phenotype, binding both hIgG2 and mIgG1. Further functionally significant mutations in human Fcγ receptors and possible novel mechanisms for inherited differences in disease susceptibility should be sought with unbiased screening methods.

scholarly journals Differential binding properties of [3H]dextrorphan and [3H]MK-801 in heterologously expressed NMDA receptors

2005 ◽  
Vol 49 (1) ◽  
pp. 1-16 ◽  
Author(s):  
K.T. LePage ◽  
J.E. Ishmael ◽  
C.M. Low ◽  
S.F. Traynelis ◽  
T.F. Murray
Keyword(s):  
Nmda Receptors ◽  
Binding Properties ◽  
Mk 801 ◽  
Differential Binding
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