Chapitre 9 La culture in vitro

2021 ◽  
pp. 111-122
Keyword(s):  
Author(s):  
Pengfei Wu ◽  
Xin Wang ◽  
Lilan Gao ◽  
Chunqiu Zhang

1982 ◽  
Vol 220 (2) ◽  
pp. 219-225 ◽  
Author(s):  
Yu-Jui Wan ◽  
Tsung-Chieh Wu ◽  
Ivan Damjanov

In Vitro ◽  
1977 ◽  
Vol 13 (11) ◽  
pp. 806-807 ◽  
Author(s):  
Ram S. Verma ◽  
Carole Rubenstein ◽  
Harvey Dosik

2010 ◽  
Vol 3 (5) ◽  
pp. 419-453
Author(s):  
B. Ubertini ◽  
L. Nardelli ◽  
S. Barei ◽  
G. Santero
Keyword(s):  

1979 ◽  
Vol 177 (2) ◽  
pp. 559-567 ◽  
Author(s):  
C S Heng-Khoo ◽  
R B Rucker ◽  
K W Buckingham

Evidence is presented for the presence of precursor to tropoelastin in chick arterial extracts. The precursor is approx. 100 000 daltons in size. It is suggested to be a precursor to tropoelastin (72 000 daltons). This protein may be observed in culture in vitro if appropriate precautions are taken to inhibit proteolysis. Once synthesized, it appears to be converted into tropoelastin within 10–20 min. The protein may also be detected in vivo. When 1-day-old cockerels were fed on a copper-deficient diet (less than 1 p.p.m. to inhibit cross-linking) containing epsilon-aminohexanoic acid (0.2%) to retard proteolysis and then injected wiht [3H]valine, extraction of arterial proteins 12h after injection resulted in detection of two major peaks of [3H]valine-labelled protein with pI values of pH 7.0 and 5.0 respectively. The protein that focused at pH 7.0 was estimated to be about 100 000 daltons in size and could be shown to be converted into a more basic protein with the properties of tropoelastin. It is speculated that the protein with pI 5.0 may be yet another extension peptide. The data appear to be in keeping with similar observations by ourselves and others that a proform of tropoelastin exists, and, in at least one step before conversion into tropoelastin, exists as a 100 000-dalton protein subunit.


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