scholarly journals The origin of N-terminal residues in acetic acid-soluble calf-skin collagen

1962 ◽  
Vol 83 (2) ◽  
pp. 245-248 ◽  
Author(s):  
FS STEVEN ◽  
GR TRISTRAM
Keyword(s):  
1958 ◽  
Vol 108 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Jerome Gross

Precipitation (or gelation) of collagen from cold neutral salt solution induced by warming was shown to be reversible on subsequent cooling. The degree of reversibility of heat precipitation rapidly diminished with time of incubation at 37°C. For calf skin collagen (acetic acid-extracted) and guinea pig skin collagen (crude NaCl extract) in neutral salt solutions (Γ/2 = 0.45) roughly 90 per cent of newly formed gel redissolved on cooling at 2°C.; less than 20 per cent redissolved on cooling gels previously maintained at 37°C. for 24 hours. At physiologic ionic strength the same preparations exhibited much more rapid development of irreversible precipitation, but the same time dependence was clearly evident. Highly purified collagen from crude saline extracts of guinea pig skin exhibited the same phenomenon although the quantitative aspects were somewhat different.


1968 ◽  
Vol 243 (11) ◽  
pp. 2890-2898
Author(s):  
M P Drake ◽  
P F Davison
Keyword(s):  

1966 ◽  
Vol 241 (8) ◽  
pp. 1784-1789
Author(s):  
Leo D. Kahn ◽  
Lee P. Witnauer
Keyword(s):  

1965 ◽  
Vol 95 (2) ◽  
pp. 350-353 ◽  
Author(s):  
GR TRISTRAM ◽  
J WORRALL ◽  
DC STEER

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.


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