Cytokinins regulate calcium binding to a glycoprotein from fungal cells
| Autor: | H.B. LéJohn, Linda E. Cameron |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Purine
Cytological Techniques Biophysics chemistry.chemical_element Pronase Plasma protein binding Biology Calcium Biochemistry Fungal Proteins chemistry.chemical_compound Plant Growth Regulators medicine Magnesium Trypsin Binding site Molecular Biology Glycoproteins Manganese Fungal protein Adenine Calcium Radioisotopes Cell Membrane Sodium fungi Fungi Cell Biology Achlya Spores Fungal biology.organism_classification Molecular Weight chemistry Barium Strontium Potassium Colorimetry Muramidase Protein Binding medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 54:1053-1060 |
| ISSN: | 0006-291X |
| Popis: | A glycoprotein that binds about 20 atoms of Ca per mole has been purified from the osmotic shock fluid of some unicellular coenocytic water-molds, Achlya spp. and Blastocladiella emersonii . The binding of calcium is allosterically regulated by N6-(substituted)adenine derivatives, cytokinins. Pyrimidines, purine and pyrimidine nucleosides, auxins, and benzimidazole derivatives are ineffective in inhibiting calcium binding. Lysozyme partially inactivates the molecule so that a high affinity calcium binding site is destroyed. Trypsin and pronase inactivate the molecule so that Ca++ binding to both high and low affinity sites is affected. Cytokinins inhibit calcium binding to both sites. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|