Electron microscopic demonstration of acid-labile, 4D-staggered intermolecular association of collagen formed in vitro. 1985

K Kobayashi, and T Ito, and T Hoshino

The formation of acid-labile, unidirectional, and 4D-staggered dimers and polymers of collagen molecules in solutions at pH 4.0 and 4.5 has been demonstrated under the electron microscope. Collagen molecules extracted from lathyritic rat skin was dialyzed from 0.5 M acetic acid sequentially against 5-10 mM acetate buffer (pH 4-4.5) at 4 degrees C for 3-4 days, 0.3% glutaraldehyde in the same buffers for further 2 days, 0.5 M acetic acid, and then against 0.2% ATP X Na2/0.1 M acetic acid. Fibrous, unidirectional segment-long-spacing (SLS) forms were observed with 0.4D overlap between adjacent segments. Such a form was not observed when glutaraldehyde fixation step was omitted or when SLS was formed directly from the acidic solution; in both cases, monomeric SLS was only observed. It is concluded that collagen molecules, dispersed monomeric in acidic pH, form unidirectional linear dimers or polymers in which the molecules are associated with 0.4D overlap (4D stagger) at pH 4-4.5.

UI MeSH Term Description Entries
D007842 Lathyrism A paralytic condition of the legs caused by ingestion of lathyrogens, especially BETA-AMINOPROPIONITRILE or beta-N-oxalyl amino-L-alanine, which are found in the seeds of plants of the genus LATHYRUS. Neurolathyrism
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D011108 Polymers Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS). Polymer
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012867 Skin The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

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