Pub. Date : 1982 Nov 1
PMID : 6186243
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Evidence for similar conformational changes in alpha 2-macroglobulin on reaction with primary amines or proteolytic enzymes. | Amines | alpha-2-macroglobulin | Homo sapiens |
| 2 | Reactions of alpha(2)-macroglobulin (alpha(2)M) with primary amines (ammonium chloride, methylammonium chloride and ethylammonium chloride) or proteolytic enzymes (trypsin, chymotrypsin and thrombin) resulted in changes of the absorption, fluorescence and circular-dichroism spectra and of the sedimentation coefficient of the inhibitor. | Amines | alpha-2-macroglobulin | Homo sapiens |
| 3 | Reactions of alpha(2)-macroglobulin (alpha(2)M) with primary amines (ammonium chloride, methylammonium chloride and ethylammonium chloride) or proteolytic enzymes (trypsin, chymotrypsin and thrombin) resulted in changes of the absorption, fluorescence and circular-dichroism spectra and of the sedimentation coefficient of the inhibitor. | Amines | alpha-2-macroglobulin | Homo sapiens |
| 4 | All physico-chemical changes caused by the inactivation of alpha(2)M by the amines were identical with, or highly similar to, those induced by the formation of the enzyme-inhibitor complexes. | Amines | alpha-2-macroglobulin | Homo sapiens |
| 5 | The frictional ratio, calculated from the increase in sedimentation coefficient, decreased from 1.67 for untreated alpha(2)M to 1.57 for the amine- or proteinase-treated inhibitor. | Amines | alpha-2-macroglobulin | Homo sapiens |
| 6 | The circular-dichroism analyses indicated that the reaction of alpha(2)M with either amines or proteinases is accompanied by a loss of the small amount (about 5%) of alpha-helix of the untreated protein. | Amines | alpha-2-macroglobulin | Homo sapiens |