Collagen digestibility

Details of follicular formation and ovulation remain unsettled. There is some indication that the liquor is formed by filtration of plasma rather than as a result of venous or lymphatic obstruction. Increased hydrostatic pressure in the follicle is unlikely to cause its rupture. Rupture seems to result from focal alteration of the site of the stigma. Electron microscopic examination of the stimaga reveals collagen digestion and cell separation. 

Injection of an enzymatic digest of human insoluble skin collagen onto a HPLC showed a single major peak in the chromatogram when monitored by a LW fluorescence detector (Fig. 1). It was noted that the size of the peak from collagen digests prepared from age 10 and 47 year-old individuals with type 1 diabetes were comparatively more intense versus those from nondiabetic individuals of similar age Furthermore, peak area increased with chronological age and was considerably more intense in individuals with ESRD. Subsequently the peak was named LWl. 

Part of the diet consists of fats, which are triglycerol esters of fatty acids (FAs). The FAs from digestion of ingested fats can be metabolized in a variety of pathways. Fragments of the original FAs are preserved in these processes and can be utilized in the biosynthesis of other molecules. It is important to note that, during metabolism, almost all FAs are broken down into two-carbon units. The only exceptions are FAs with odd numbers of carbon atoms these are relatively rare in the diet. It ean be shown further that there is a partial barrier to the incorporation of FA-derived carbon into the amino acids which constitute collagen. 

Wu JJ and Eyre DR (1988) Fine powdering exposes the mineral-protected collagen of bone to protease digestion. Calcif Tissue Int 42, 243-247. 

The incubation conditions for trypsin and pepsin were chosen after preliminary tests showed that measurable amounts of collagen were released into the incubation solutions. In trypsin incubations, degradation is fastest on day 1 and decreasing in velocity thereafter. Slices digested extensively by pepsin were fragile. Infermittent changes of pepsin solutions were therefore avoided. 

Emission spectra of buffer-exposed (B) and glucose-exposed (G) dentin collagenolysates. 200 pmol of digested collagen in 3 ml buffer pH 7.4, scanspeed 3.6 nm/s. 

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