scholarly journals The influence of N-acetylneuraminic acid on the properties of human orosomucoid

1986 ◽  
Vol 236 (1) ◽  
pp. 149-153 ◽  
Author(s):  
M L Friedman ◽  
J R Wermeling ◽  
H B Halsall
Keyword(s):  
Thermal Stability ◽  
Biological Activity ◽  
Fluorescence Spectroscopy ◽  
Ligand Binding ◽  
Protein Conformation ◽  
Acid Content ◽  
Acetylneuraminic Acid ◽  
Water Of Hydration ◽  
Hydrophobic Binding ◽  
A Charge

Little is known of the relationships that may exist among the three principal functionalities of glycoproteins. Orosomucoids of closely defined N-acetylneuraminic acid content were examined for evidence of influence of N-acetylneuraminic acid content on the physical properties of the glycoprotein. Fluorescence spectroscopy gave no indication of conformational change in the protein core upon desialylation. Small changes in the chromatographic partition coefficient, sigma, and thermal stability, Td, are interpreted to reflect loss of water of hydration and increased glycan stem-protein interaction without a major repositioning of the chains. Ligand-binding measurements indicate no alteration in the hydrophobic binding domain and a possible interaction between chlorpromazine and N-acetylneuraminic acid. All changes seen are progressive and occur through a region where changes in biological activity are not found. It is suggested that the dependence of biological activity on N-acetylneuraminic acid content in orosomucoid reflects, not coupled changes in protein conformation, but a charge-density-related interaction such that, below a contribution of four or five N-acetylneuraminic acid residues, activity is modified.

Synthesis and Axial-Ligand Binding of Zinc Complexes of Amphiphilic Porphyrins Containing a Hydrophobic Binding Pocket

1997 ◽  
Vol 26 (8) ◽  
pp. 819-820 ◽  
Author(s):  
Hiroyasu Imai ◽  
Hiroki Munakata ◽  
Atsuko Takahashi ◽  
Shigeo Nakagawa ◽  
Yoshio Uemori
Keyword(s):  
Ligand Binding ◽  
Binding Pocket ◽  
Axial Ligand ◽  
Zinc Complexes ◽  
Hydrophobic Binding

scholarly journals Ligand Binding and Signaling of HARE/Stabilin-2

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 273 ◽  
Author(s):  
Edward N. Harris ◽  
Fatima Cabral
Keyword(s):  
Biological Activity ◽  
Hyaluronic Acid ◽  
Cell Surface ◽  
Ligand Binding ◽  
Antisense Oligonucleotides ◽  
External Environment ◽  
Scavenger Receptors ◽  
Extracellular Material ◽  
Synthetic Drugs ◽  
Multiple Ligands

The Stabilin receptors are a two-member family in the type H class of scavenger receptors. These dynamic receptors bind and internalize multiple ligands from the cell surface for the purpose of clearing extracellular material including some synthetic drugs and for sensing the external environment of the cell. Stabilin-1 was the first receptor to be cloned, though the biological activity of Hyaluronic Acid Receptor for Endocytosis (HARE)/Stabilin-2 was observed about 10 years prior to the cloning of Stabilin-1. Stabilin-1 has a more diverse expression profile among the tissues than HARE/Stabilin-2. This review will focus on HARE/Stabilin-2 and its interactions with hyaluronan, heparin, and phosphorothioate antisense oligonucleotides and what is known about how this receptor participates in signaling upon ligand binding.

scholarly journals A series of Mn(i) photo-activated carbon monoxide-releasing molecules with benzimidazole coligands: synthesis, structural characterization, CO releasing properties and biological activity evaluation

RSC Advances ◽  
2019 ◽  
Vol 9 (36) ◽  
pp. 20505-20512 ◽  
Author(s):  
Mixia Hu ◽  
YaLi Yan ◽  
Baohua Zhu ◽  
Fei Chang ◽  
Shiyong Yu ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Biological Activity ◽  
Activated Carbon ◽  
Fluorescence Spectroscopy ◽  
Single Crystal ◽  
Structural Characterization ◽  
X Ray Diffraction ◽  
X Ray ◽  
H Nmr ◽  
C Nmr

Five Mn(i) photo-activated carbon monoxide-releasing molecules were synthesized by reactions of MnBr(CO)5 with L1–L4, and characterized via single crystal X-ray diffraction, 1H-NMR, 13C-NMR, IR, UV-vis and fluorescence spectroscopy.

Binding of Radiolabeled Folate and 5-Methyltetrahydrofolate to Cow's Milk Folate Binding Protein at pH 7.4 and 5.0. Relationship to Concentration and Polymerization Equilibrium of the Purified Protein

2001 ◽  
Vol 21 (6) ◽  
pp. 733-743 ◽  
Author(s):  
Jan Holm ◽  
Steen Ingemann Hansen
Keyword(s):  
Ligand Binding ◽  
Binding Affinity ◽  
Conformational Changes ◽  
Protein Conformation ◽  
Binding Protein ◽  
Cow’S Milk ◽  
Folate Binding Protein ◽  
Cow's Milk ◽  
Polymerization Equilibrium ◽  
Methyl Tetrahydrofolate

Binding of folate (pteroylglutamate) and 5-methyltetrahydrofolate, the major endogenous form of folate, to folate binding protein purified from cow's milk was studied at 7°C to avoid degradation of 5-methyltetrahydrofolate. Both folates dissociate rapidly from the protein at pH 3.5, but extremely slowly at pH 7.4, most likely due to drastic changes in protein conformation occurring after folate binding. Dissociation of 5-methyltetrahydrofolate showed no increase at 37°C suggesting that protein-bound-5-methyltetrahydrofolate is protected against degradation. Binding displayed two characteristics, positive cooperativity and a binding affinity that increased with decreasing concentrations of the protein. The binding affinity of folate was somewhat greater than that of 5-methyl tetrahydrofolate, in particular at pH 5.0. Ligand-bound protein exhibited concentration-dependent polymerization (8-mers formed at 13 μM) at pH 7.4. At pH 5.0, only folate-bound forms showed noticeable polymerization. The fact that folate at pH 5.0 surpasses 5-methyltetrahydrofolate both with regard to binding affinity and ability to induce polymerization suggests that ligand binding is associated with conformational changes of the protein which favor polymerization.

scholarly journals Membrane Fluidity Modulates Thermal Stability and Ligand Binding of Cytochrome P4503A4 in Lipid Nanodiscs

Biochemistry ◽  
2016 ◽  
Vol 55 (45) ◽  
pp. 6258-6268 ◽  
Author(s):  
Wynton D. McClary ◽  
John P. Sumida ◽  
Michele Scian ◽  
Lorela Paço ◽  
William M. Atkins
Keyword(s):  
Thermal Stability ◽  
Ligand Binding ◽  
Membrane Fluidity ◽  
Lipid Nanodiscs
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