Example sentences of "[noun pl] of [art] α " in BNC.

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1 As described previously , Β 1 integrins on the cell surface of untreated cells migrate under non-reducing conditions as three major bands : a strong signal averaging at 115 KD representing the mature Β 1 subunit , a broad signal between 140–160 KD at postions of the α 2 , α 6 , and α v chains , and a weak signal at 200 KD of the α 1 chain ( Fig 3 ) .
2 Inclusion of an additional 25 amino acids on alternative forms of the α subunit could lead to further diversification of nicotinic receptors of muscle as has been noted in other ionic channels , most notably in shaker class of K channel from Drosophila ( 20 ) , and N-methyl-D aspartate ( NMDA ) receptor in rat brain ( 20a ) .
3 Pretreatment of human colon adenocarcinoma derived HT-29 cells with DMJ resulted in an expression of the 105 kD β 1 precursor chain and of smaller forms of the α 1 , α 3 , α 6 , and α v integrin subunits in a time and dose dependent manner .
4 Sargent ( 1979 ) generalizes the model to the case in which : with the unrestricted VAR : In this case the restrictions on the γ i 's and the δ i 'S in equation ( 3.51b ) are complicated non-linear functions of the α i 's and β i 's .
5 The complete integrin consists of a head or ligand binding region made up of both the N terminal regions of the α and Β subunits ; a body which incorporates a hydrophobic membrane spanning domain , and two cytoplasmic linked domains .
6 To analyze the expression of the two variants of the α subunit in human skeletal muscle and in non-muscle tissues , we used cDNA from human skeletal muscle , the rhabdomyosarcoma cell line TE671 , and human brain , heart , kidney , liver , lung and thymus. 5' and 3' primers spanning the α subunit 's extracellular region , including the P3A exon were used to analyze α subunit expression .
7 In the latter cells , PLC- β1 , but not PLC- γ1 or PLC- 1 , may be activated by members of the α q -subfamily of the G protein α- subunits .
8 Clearly , PLC- β1 is activated by all four members of the α q family ( α q , α 11 , α 14 , and α 16 ) .
9 In fact holoenzymes reconstituted in vitro with truncated α-subunits , α-235 or α-256 , containing respectively the first 235 and 256 amino acids of the 329 residues of the α protein were perfectly able to initiate transcription at constitutive promoters , but were unable to respond to CRP activation at type I promoters [ 13 ] .
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