Cuticle structure and composition of two invertebrates of hydrothermal vents: Alvinella pompejana and Riftia pachyptila

The structure of the cuticle from the "Pompeii worm" Alvinella pompejana and Riftia pachyptila is presented. The cuticle structure of Alvinella is similar to that of other annelid species, whereas that of Riftia presents patterns which are observed in biological analogues of cholesteric liquid crystals. The amino acid composition of a vestimentiferan cuticle is presented for the first time and compared with that of other invertebrates

High-angle electron diffraction of frozen hydrated collagen.

By using the techniques developed by Taylor et al. [(1975) J. Mol. Biol. 92, 165-167] (freezing of the hydrated specimen before its insertion into the electron microscope and keeping it frozen throughout the diffraction experiment), it was possible to obtain a high-angle electron-diffraction pattern from collagen fibrils. This pattern is in good agreement with that obtained by high-angle X-ray diffraction. Electron diffraction will be very useful to study collagen, because the diffraction pattern from a carefully selected area of one fibril is now feasible

Further biochemical and physicochemical characterization of minor disulfide-bonded (type IX) collagen, extracted from foetal calf cartilage.

International audienceMinor disulfide-bonded collagen (previously termed X1-X7 and now called type IX collagen) was isolated from foetal calf cartilage after pepsin treatment. At least three native fractions, containing, respectively, the X1X2X3, X4, and X5X6X7 chains, were separated; and from further biochemical and physicochemical experiments (differential scanning calorimetry, electrical birefringence, rotary shadowing), we propose a tentative model for their organization within a parent molecule. X1 and X2 are molecules composed of three chains of apparent Mr 62,000 and 50,000 linked by interchain disulfide bonds and containing pepsin-sensitive regions. The cleavage of at least three of these sites, present within X2, gives rise to the X3 and X5X6X7 fractions composed of molecules 80-100 nm and 40-55 nm in length, respectively. The X5X6X7 fraction is not digested by pepsin at 30 degrees C owing to its high thermal stability (certainly explained by its high hydroxyproline + proline content). This organization is in good accordance with that proposed for chicken cartilage type IX collagen; differences could only exist in the number and (or) the location of the pepsin-sensitive sites.Minor disulfide-bonded collagen (previously termed X1-X7 and now called type IX collagen) was isolated from foetal calf cartilage after pepsin treatment. At least three native fractions, containing, respectively, the X1X2X3, X4, and X5X6X7 chains, were separated; and from further biochemical and physicochemical experiments (differential scanning calorimetry, electrical birefringence, rotary shadowing), we propose a tentative model for their organization within a parent molecule. X1 and X2 are molecules composed of three chains of apparent Mr 62,000 and 50,000 linked by interchain disulfide bonds and containing pepsin-sensitive regions. The cleavage of at least three of these sites, present within X2, gives rise to the X3 and X5X6X7 fractions composed of molecules 80-100 nm and 40-55 nm in length, respectively. The X5X6X7 fraction is not digested by pepsin at 30 degrees C owing to its high thermal stability (certainly explained by its high hydroxyproline + proline content). This organization is in good accordance with that proposed for chicken cartilage type IX collagen; differences could only exist in the number and (or) the location of the pepsin-sensitive sites