scholarly journals Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.

1992 ◽  
Vol 89 (16) ◽  
pp. 7467-7470 ◽  
Author(s):  
K. Vuori ◽  
T. Pihlajaniemi ◽  
M. Marttila ◽  
K. I. Kivirikko
2018 ◽  
Vol 60 (12) ◽  
pp. 924-934 ◽  
Author(s):  
Yoshiki Morifuji ◽  
Jian Xu ◽  
Noriko Karasaki ◽  
Kazuhiro Iiyama ◽  
Daisuke Morokuma ◽  
...  

1995 ◽  
Vol 4 (12) ◽  
pp. 2587-2593 ◽  
Author(s):  
Johan Kemmink ◽  
Nigel J. Darby ◽  
Thomas E. Creighton ◽  
Klaas Dijkstra ◽  
Ruud M. Scheek

Gene ◽  
2006 ◽  
Vol 366 (2) ◽  
pp. 209-218 ◽  
Author(s):  
M. Ciaffi ◽  
A.R. Paolacci ◽  
E. D'Aloisio ◽  
O.A. Tanzarella ◽  
E. Porceddu

2020 ◽  
Vol 63 (18) ◽  
pp. 10263-10286 ◽  
Author(s):  
Andrea Shergalis ◽  
Ding Xue ◽  
Fatma Z. Gharbia ◽  
Hannah Driks ◽  
Binita Shrestha ◽  
...  

1992 ◽  
Vol 286 (3) ◽  
pp. 819-824 ◽  
Author(s):  
K Rose ◽  
G Turcatti ◽  
P Graber ◽  
S Pochon ◽  
P O Regamey ◽  
...  

The purification to homogeneity of an active soluble 25 kDa fragment of CD23, produced in insect cells using the baculovirus expression system, is described. Peptide mapping and analysis by Edman degradation and mass spectrometry permitted partial characterization of the protein. A total of 165 out of 172 residues, including N-terminal and C-terminal regions, were mapped. The positions of the two disulphide bonds in the IgE-binding region were also determined: residue 110 is joined to residue 124, and residue 42 to residue 133. Natural CD23 25 kDa fragment was also analysed and found to possess the same disulphide bond arrangement. These results extend the previously noted sequence similarity with lectins to elements of secondary structure.


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