Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “AMINOPROPIONITRILE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 523 records · Page 29Linked to original sources

Type I collagen-phosphophoryn interactions: specificity of the monomer-monomer binding.

It has been postulated that phosphophoryn (PP) molecules bind specifically to type I collagen fibrils as the key event in inducing matrix mineralization in dentin. The nature and specificity of the collagen molecule-PP interaction has been examined by rotary shadowing-electron microscopy of mixtures of native, monomeric lathyritic rat skin collagen and purified rat incisor PP. An antibody to the amino-telopeptide of the collagen alpha1(I)-chain was used to determine the N-terminal end of the collagen molecules. Solutions of collagen and PP in 0.01 M ammonium formate (+/- antibody) were mixed and spread in 70% glycerol-30% 0.01 M ammonium formate on freshly cleaved mica surfaces using the sandwich technique. After rotary shadowing with Pt and backcoating with a carbon film, the spreads were viewed in a JEOL 1200EX TEM. The PP appeared as 15-nm diameter globules, the collagen as semi-flexible 270 nm filaments. At neutral pH and low PP/collagen mixing ratios, a single interaction site was evident, centered at approximately 210 nm from the N-terminus. The binding interaction induced a local conformational change in the collagen, bending the molecule and reducing its effective length. The sequence within the collagen-PP-binding domain has a net-positive charge but contains both positively and negatively charged groups.

Amino Acid Sequence↗

Correlation of high-speed tensile strength with collagen content in control and lathyritic rat skin.

Severity of lacerative skin injury depends on the applied load and the resistance of the tissue. At low (static) rates of loading there is a high degree of correlation between skin tensile strength and the degree of collagen crosslinking, with little added strength due to collagen interactions with the glycosaminoglycan matrix. We examined the effects of high (ballistic) rates of loading in order to determine the contributions to strength made by both the degree of collagen crosslinking and the collagen-matrix interaction. Tensile failure experiments were conducted using the dorsal skin of rats 1.5-6 months of age. Test specimen orientations were cut parallel and transverse to the body axis at cephalad and caudad locations on the dorsum. Tensile strength was measured at nominal strain rates of 30%/sec (low speed) and 6000%/sec (high speed) using both control and lathyrogen fed rats. Biochemical analyses were conducted to determine the amount of total and crosslinked (insoluble) collagen. In low-speed tests, there was a significant correlation (r > or = 0.900) between collagen content and skin tensile strength measured both transverse and parallel to the spine. The degree of correlation was higher with insoluble (r = 0.973) collagen content than with total (r = 0.901) collagen. The effect of a lathyrogen diet produced a significant (P < 0.001) reduction (two- to threefold) in tensile strength compared to control. In both high- and low-speed groups, tensile strength was greatest in the transverse samples with a significant correlation to collagen content (r > or = 0.858).(ABSTRACT TRUNCATED AT 250 WORDS)

Aminopropionitrile↗

Proteolysis of tropoelastin.

The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.

Aminopropionitrile↗

Chronic lathyrism and atheromatosis in the rat. Study of the V.L.D.L. and plasma and arterial wall lipids.

Temporary chronic administration of Beta-amino-propionitrile (B.A.P.N.) produced morphological and biochemical changes of the aortic wall of rat as well as abnormalities of the plasma lipid levels. A hyperlipidic diet resulted in the blood plasma lipid abnormalities as B.A.P.N. intoxication. Nine weeks of B.A.P.N. followed by 42 weeks of a hyperlipidic diet increased the aortic cholesterol level and induced an atheroma. The diet alone produced only an endothelial lipid overload. The structure of arterial wall played the decisive role in atherogenesis.

Aminopropionitrile↗

Quantum chemical study of relative reactivities of a series of amines and nitriles: relevance to prebiotic chemistry.

Using the Iterative Extended Hucken Theory (IEHT) calculations of the elctron distribution and orbital energies of a series of thirteen amines, nitriles and amino-nitriles relevant to prebiotic and cosmo-chemistry have been carried out. Ground state properties such as the energy and nature of the highest occupied (HOMO) and lowest empty (LEMO) molecular orbitals, net atomic charges and number of non-bonding electrons have been identified as criteria for correlating the relative nucleophilicity of amine and nitrile nitrogens and the electrophilicity of nitrile and other unsaturated carbon atoms. The results of such correlations can be partially verified by known chemical behavior of these compounds and are used to predict and understand their role in prebiotic organic synthesis.

Amines↗

Influence of beta-aminoproprionitrile (BAPN) on cell growth and elastic fiber formation in cultures of auricular chondrocytes.

Auricular chondrocytes isolated from 4-day-old rabbits and grown in vitro for 14 days, proliferated rapidly and produced a conspicuous network of elastic fibers. Beta-aminoproprionitrile (BAPN), which in vivo inhibits cross-linking of elastin, decreased the formation of elastic fibers at a concentration of 10-20 micrograms/ml and prevented formation at 40 micrograms/ml. At a concentration of 5 micrograms/ml only the so-called patches of elastin appeared to be absent. The inhibitory effect of BAPN on cell growth did not exceed 10%, which indicates that BAPN is only slightly harmful to auricular chondrocytes and can safely be used in studies on elastin deposition by these cells in vitro.

Aminopropionitrile↗