Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine achilles tendon collagen type I

Chemosphere ◽  
2007 ◽  
Vol 67 (8) ◽  
pp. 1618-1627 ◽  
Author(s):  
C.S. Ku ◽  
M. Sathishkumar ◽  
S.P. Mun
2016 ◽  
Vol 44 (8) ◽  
pp. 1998-2004 ◽  
Author(s):  
Sebastian A. Müller ◽  
Lutz Dürselen ◽  
Patricia Heisterbach ◽  
Chris Evans ◽  
Martin Majewski

2019 ◽  
Vol 13 (5) ◽  
pp. 874-891 ◽  
Author(s):  
Fauzi Mh Busra ◽  
Nor Fadilah Rajab ◽  
Yasuhiko Tabata ◽  
Aminuddin B. Saim ◽  
Ruszymah B.H. Idrus ◽  
...  

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.


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