. Author manuscript; available in PMC: 2007 Dec 1.

Published in final edited form as: Biochem Biophys Res Commun. 2006 Oct 5;350(4):1032–1037. doi: 10.1016/j.bbrc.2006.09.147

Table 1.

Structural parameters of collagen XVII recombinant proteins

	Average Stoke’s radius (nm)
Recombinant proteins	Trimer	Monomer	sedimentation coefficient	Axial ratio (P)
sec180	13.6 +/− 0.4	9.1 +/− 0.6	5.3 +/− 0.2	63
sec180- N16	14.3	9.0	5.5 +/− 0.4	81
sec180-trunc	10.3 +/− 0.07	5.1 +/− 0.4	2.6	79
sec180-trunc-cHis	11.2	5.3
trunc- N16-cHis	undetectable	4.5 +/− 0.3

The Stoke’s radius of each protein was determined from gel filtration chromatographic data (see Figure 4), and the sedimentation coefficient was obtained from glycerol gradient sedimentation profiles. The axial ratio was calculated as described in the text. Each result represents the average of 2 to 5 runs. The standard deviation is given only when at least 3 runs were performed.