Molecular weight collagen

Finally, the possibility that not only surface adsorption but also penetration of peptides into the hair fiber and deposition in the cortex could occur is supported by a study carried out by Cooperman and Johnson (101). Low-molecular-weight collagen peptides were found to be absorbed on both virgin and damaged hair, but the low-specific-detection... 

A possible assay may be based on disc gel electrophoresis of meat extracts, prepared in the presence of urea and SDS. The band intensities of the lower molecular weight collagen fragments increase in proteinase-treated meat. 

Table 2. Survey of synthesized collagen models. Average molecular weights (M)... 

Gel filtration on Sephadex G 25, G 50 or G 75 beads was just available. After standardization with peptides and proteins of known length, the molecular weight of the respective fraction could be determined. Also cyanogen bromide peptides of collagen chains were available in the later sixties, thus leading to a more consistent standardization15"17. ... 

Vierboom MP, Zavodny PJ, Chou CC, et al. Inhibition of the development of collagen-induced arthritis in rhesus monkeys by a small molecular weight antagonist of CCR5. Arthritis Rheum 2005 52(2) 627-636. 

The individual collagen ropes are called fibrils, and have an average molecular weight of around 300 000 Daltons (atomic mass units), with a length of 260 nm and a diameter of 1.4-2.0 nm. In the collagen fibres which can be seen... 

Chromatographic purification of cross-links. The initial steps of the purification were to separate the cross-links from monomeric amino acids, followed by the separation of individual cross-links. The acid hydrolyzate of demineralized roof powder (13.0 g collagen) was separafed on a size exclusion column fo yield the high molecular weight fractions. 

V-1 from acid and alkaline hydrolyzates, SCX-HPLC of amino acids, a mixture of purified crosslinks and hydroxylysine b purified cross-link V-2 c amino acids from an acid hydrolyzate (6 M HCl) of reduced bovine dentin retained on a phenylboronate agarose column after purification as high molecular weight fractions by repeated size exclusion chromatography d as c, alkaline hydrolyzate (2 M KOH). Injections (c, d) resulted from 18 and 52 mg collagen originally hydrolyzed, respectively. 1 = 111 (HP) 2 = V-2 3 = IV 4 = V-1-1 (DHLNL) 5 = HLNL (bovine tendon) 6 = VI (histidinoalanine ) 7 = hydroxylysine 8 = VI (lysinoalanine). 

---