The bronchial tree and lobular division of the lung of the white handed gibbon

The bronchial tree and lobular division of the lungs of four white handed gibbons (Hylobates agilis) were examined from the viewpoint of comparative anatomy, based upon the fundamental structure of the bronchial ramifications of the mammalian lung (Nakakuki, 1975, 1980). The right lung of the white handed gibbon consists of the upper, middle, lower, and accessory lobes, whereas the left lung consists of the middle and lower lobes. Each lobe is separated by the interlobular fissure, on both sides. The right and left lungs have the dorsal bronchiole system, lateral bronchiole system, and ventral bronchiole system. The medial bronchiole system is lacking on both sides. In the right lung, the upper lobe is formed by the first branch of the dorsal bronchiole system. The middle lobe is formed by the first brach of the lateral bronchiole system, and the accessory lobe by the first branch of the ventral bronchiole system. The remaining bronchioles constitute the right lower lobe. In the left lung, the upper lobe bronchiole, which is the first branch of the dorsal bronchiole system, is lacking. Therefore, the middle lobe bronchiole, i.e. the first branch of the lateral bronchiole system, is well developed. The accessory lobe bronchiole, the first branch of the ventral bronchiole system, is also lacking. The remaining bronchioles constitute the left lower lobe. These features were compared with those of other apes and man.     

Paradoxical effect of sudan III on the in vivo and in vitro genotoxicity elicited by 7,12-dimethylbenz(a)anthracene

Effect of the induction of drug metabolizing enzymes by Sudan III on the in vivo and in vitro genotoxicity elicited by 7,12-dimethyl-benz(a)anthracene (DMBA) was investigated. A significant suppression of DMBA-induced micronucleated reticulocytes was observed in C57BL/6 mice treated with Sudan III intraperitoneally for 3 or 5 days before injection of the DMBA. However, the preincubation of DMBA with hepatic microsomes from Sudan III-treated rats caused a marked increase in the in vitro mutagenicity in the Ames assay, paradoxically. Sudan III was found to induce CYP 1A1, 7-ethoxycoumarin O-deethylase activity as well as both UDP-glucuronyl transferase and glutathione S-transferase activities. The increase of mutagenicity of DMBA observed in the Ames assay using hepatic microsomes from Sudan III-treated rats was inhibited by the addition of uridine 5′-diphosphoglucuronic add or reduced glutathione with cytosol. Mutagenic metabolites of DMBA formed by CYP1A1 appeared to be effectively detoxified by these phase II enzymes. The results of this study suggest that Sudan III-induced prevention of in vivo mutagenesis is due to the induction of both CYP 1A1 and detoxifying phase II enzymes. The induced CYP1A1 may accelerate formation of active metabolic intermediates, but phase II enzymes are also induced and detoxify these intermediates to inactive metabolites. This would reduce residence time of the carcinogen in the body and the time of exposure to active metabolites for target organs.     

The bronchial tree and lobular division of the gorilla lung

The bronchial ramification in one specimen of gorilla lung was examined from the viewpoint of comparative anatomy, on the basis of the fundamental structure of bronchial ramification in the mammalian lung (Nakakuki, 1975, 1980). The right lung of the gorilla consists of the upper, middle, lower, and accessory lobes. The right lung has the dorsal, lateral, and ventral bronchiole systems, but the medial bronchiole system is lacking. The upper lobe is formed by the first branch of the dorsal bronchiole system. The middle lobe is formed by the first branch of the lateral bronchiole system. The accessory lobe is formed by the first branch of the ventral bronchiole system. The remaining bronchioles constitute the lower lobe. The left lung consists of the middle and lower lobes; the upper and accessory lobes are lacking. The left lung has the dorsal and lateral bronchiole systems, but the ventral and medial bronchiole systems are lacking. The middle lobe is formed by the first branch of the lateral bronchiole system. The remaining bronchioles constitute the lower lobe. The bronchial ramifications of the gorilla lung are rather similar to those of the human lung.     

Action of Pseudomonas isoamylase on various branched oligo- and poly-saccharides

Pseudomonas isoamylase (EC 3.2.1.68) hydrolyzes (1 → 6)-α-D-glucosidic linkages of amylopectin, glycogen, and various branched dextrins and oligosaccharides. The detailed structural requirements for the substrate are examined qualitatively and quantitatively in this paper, in comparison with the pullulanase of Klebsiella aerogenes. As with pullulanase. Ps. isoamylase is unable to cleave D-glucosyl stubs from branched saccharides. Ps. isoamylase differs from pullulanase in the following characteristics: (1) The favored substrates for Ps. isoamylase are higher-molecular-weight polysaccharides. Most of the branched oligosaccharides examined were hydrolyzed at a lower rate, 10% or less of the rate of hydrolysis of amylopectin. (2) Maltosyl branches are hydrolyzed off by Ps. isoamylase very slowly in comparison with maltotriosyl branches. (3)Pr. isoamylase requires a minimum of three D-glucose residues in the B- or C-chain.     

Purification and some properties of Bacillus macerans cycloamylose (cyclodextrin) glucanotransferase

Bacillus macerans cycloamylose (cyclodextrin) glucanotransferase (EC 2.4.1.19) was purified by the technique of starch adsorption and DEAE-cellulose column chromatography, and then crystallized from an ammonium sulfate solution containing mM calcium chloride. The crystals of the enzyme were rod-shaped and showed a single band by disc-gel electrophoresis. The purified enzyme was dissociated into two subunits by sodium dodecyl sulfate-disc electrophoresis. The subunits had no enzyme activity. Details of each purification step and some properties of the enzyme are described in this paper.     

Minireview: Calcium-dependent proteolysis in living cells

Calcium ion, one of the second messengers in living organisms, has various functions including the ability to enhance intracellular proteolysis. This calcium-dependent proteolysis occurs in the cytosol or membrane rather than in the lysosome. Its mode of action is very wide, including cleavage of hormone receptors, activation of regulatory enzymes and limited proteolysis of the cytoskeletal structure. Although contradictory, the biochemical evidence implies a specified regulatory function of it in the cell. The activation mechanism of a purified calcium-dependent proteinase ( EC 3.4.22.- ) is also discussed.     

Reversible and irreversible conversion between the intermolecular β-structure and the disordered state of poly(s-carboxymethyl-l-cysteine) in aqueous media

Conversion between the intermolecular β-structure and the disordered state of a fractionated low molecular weight sample of poly(S-carboxyniethyl-L-cysteine) was examined mainly by the measurements of circular dichroism in the absence of salt as well as in the presence of 20 mM NaClO₄, or NaCl. In 20 mM NaClO₄ or NaCl solutions, the conversion was reversible. Under this condition, it was confirmed by direct and unambiguous evidence provided from the viscosity and the reduced scattering intensity that the β-structure was formed by intermolecular association. At low degrees of neutralization, the pH increased on dilution while it remained constant over a wide range of concentration at a high degree of neutralization. In the absence of salt, the conversion was often irreversible with respect to a concentration change at a constant degree of neutralization or to a change in the degree of neutralization at a constant concentration. The extent of the irreversible conversion decreased with the amount of β-structure in the solution. The dissociation of aggregates was very slow at low ionic strengths. It was inferred that the irreversible nature of the conversion arose from this slow dissociation of aggregates.