Biomaterial Database

alpha 2-Macroglobulin bait region integrity. Role in determining fast-form structure. 1993

P G Gettins, and J M Beechem, and B C Crews

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.

To determine whether integrity of the bait region affects the structure of the remainder of human alpha 2-macroglobulin (alpha 2M), we have determined the separation between cysteine residues in a methylamine-reacted fast-form of alpha 2M. From reduction in fluorescence intensity of covalently-bound donor fluorophore caused by proximity to an acceptor, a separation of 35 +/- 8 A was calculated, which is identical to a previously determined value for proteinase-treated fast-form alpha 2M. This indicates that although bait region cleavage is the physiological route to conformational change in alpha 2M, bait region integrity per se does not significantly affect the structure of fast-form alpha 2M.

UI	MeSH Term	Description	Entries
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D003545	Cysteine	A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.	Cysteine Hydrochloride,Half-Cystine,L-Cysteine,Zinc Cysteinate,Half Cystine,L Cysteine
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000511	alpha-Macroglobulins	Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.	Slow alpha 2-Macroglobulins,alpha 2-Acute Phase Globulins,alpha-Macrofetoproteins,45S RNP,Acute-Phase alpha 1-Protein,Slow alpha 2-Globulin,alpha 1-Acute Phase Globulin,alpha 1-Acute Phase Protein,alpha 1-Macroglobulin,alpha 2-Acute Phase Globulin,alpha-Macrofetoprotein,Acute Phase alpha 1 Protein,RNP, 45S,Slow alpha 2 Globulin,Slow alpha 2 Macroglobulins,alpha 1 Acute Phase Globulin,alpha 1 Acute Phase Protein,alpha 1 Macroglobulin,alpha 1-Protein, Acute-Phase,alpha 2 Acute Phase Globulin,alpha 2 Acute Phase Globulins,alpha 2-Globulin, Slow,alpha 2-Macroglobulins, Slow,alpha Macrofetoprotein,alpha Macrofetoproteins,alpha Macroglobulins
D013050	Spectrometry, Fluorescence	Measurement of the intensity and quality of fluorescence.	Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence
D014961	X-Ray Diffraction	The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Xray Diffraction,Diffraction, X-Ray,Diffraction, Xray,Diffractions, X-Ray,Diffractions, Xray,X Ray Diffraction,X-Ray Diffractions,Xray Diffractions