Effect of parasympathetic denervation on acetylcholine levels in the rat parotid gland. Is there an extraneuronal pool of acetylcholine?

Parasympathetic denervation of the rat parotid gland by avulsion of the auriculotemporal nerve caused a marked and lasting decrease in gland weight. Parasympathectomy did not change the levels of choline in the gland but decreased by 60% the levels of acetylcholine (ACh) ten days after surgery and 65% at 28 days. It is puzzling that relatively high levels of ACh remained after parasympathetic denervation. The presence of additional cholinergic nerves that innervate the gland, or pass through it en route to other structures may account for some of the remaining ACh. Also, Schwann cells from denervated nerves might have contributed to some of the ACh. The existence of an extraneuronal source of ACh is considered.     

Progesterone transformations as a diagnostic feature in the generaAlternaria,Stemphylium andCladosporium

Various species of the generaAlternaria, Stemphylium andCladosporium were shown to display a specific reaction characteristic for the given genus. In theAlternaria genus this is a 1-2-dehydrogenation of the A ring of the steroid molecule, inStemphylium 14α-hydroxylation and inCladosporium 7β-hydroxylation. This chemotaxonomic feature may supplement morphological and functional criteria in the taxonomy of filamentous fungi (Hyphomycetes).     

Purification and characterization of beta-glucosidase of Alcaligenes faecalis

A cellobiose-utilizing bacterium isolated from sugar cane bagasse and identified as a strain of Alcaligenes faecalis (ATCC 21400) produced an inducible beta-glucoside-splitting enzyme. The enzyme was purified by a series of streptomycin and ammonium sulfate fractionations and by Sephadex and diethylaminoethyl column chromatography. The final preparation was purified 130-fold, with a recovery of about 10% of the initial enzyme activity. The enzyme had a wide pH range, with optimal activity at pH 6.0 to 7.0. The enzyme was stable in solution at pH 6.5 to 7.8 when kept at 30 C for 2 hr, but it was destroyed by temperatures above 55 C. At 58 and 60 C, the time required to inactivate 90% of the initial activity was 16 and 6.5 min, respectively. An activation energy of 9,500 cal/mole and a K(m) of 1.25 x 10(-4)m were obtained by using p-nitrophenyl beta-glucoside as a substrate. The K(i) value and hydrolysis of cellobiose by the enzyme indicated a high affinity of the enzyme for the cellobiose. The enzyme had its specificity on beta-glucosidic linkage and the rate of hydrolisis of glucosides depended upon the nature of the aglycon moiety. The inactivation studies showed the presence of sulfhydryl groups in the enzyme. The activity of the enzyme was easily destroyed by the Cu(++) and Hg(++) ions. The Michaelis-Menton relationship and the rate of heat inactivation indicated the presence of one type of noninteracting active site in the bacterial beta-glucosidase. Molecular weight of the enzyme was estimated by gel filtration (Sephadex G-200) and sucrose density gradient, and a value of 120,000 to 160,000 was obtained.     

Isolation and Characterization of a Cellulose-utilizing Bacterium

A cellulose-decomposing aerobic and mesophilic bacterium has been isolated from soils of sugar cane fields. The terminal dilution method was adapted to isolate a single clone of cellulolytic organism from closely related contaminants. The cultural and physiological characteristics of the isolate were studied, and the organism was identified as a member of the genus Cellulomonas. The isolate excreted cellulase into the menstruum, and it hydrolyzed various cellulosic materials producing cellobiose as the final breakdown product in the menstruum. When sugar cane bagasse was properly treated with alkali and heat, the organism could decompose up to 90% of the initial substrate within 5 days. Amino acid analysis of the cell crop revealed a high content of lysine, and the essential amino acid pattern compared favorably with that of Food and Agricultural Organization reference protein.     

小麦颖果果皮绿色层内同化物的合成与分配

小麦幼嫩颖果中,果皮内侧发育出由内表皮与亚表皮组成的一薄层绿色组织。显微与亚显微结构观察表明,虽绿色层只接受到自然光照的1/4～1/8,叶绿体仍能正常发育,叶绿素含量与叶绿体数量均高出旗叶。大量胞间连丝联接相邻的绿色细胞,并在一定时期形成开放的胞间通道,显然有利于同化物的快速胞间运输。离体颖果饲喂~14CO_2试验证明,新合成的同化物从绿色细胞输向胚珠。绿色层产生的同化物可能通过合点端的珠心进入胚乳或通过珠孔直接汇聚到胚珠和分化中的原胚。     

Inositol 1,4,5-trisphosphate-induced calcium release in the organelle layers of the stratified, intact egg of Xenopus laevis

Using double-barreled, Ca2(+)-sensitive microelectrodes, we have examined the characteristics of the Ca2+ release by inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) in the various layers of Xenopus laevis eggs in which the organelles had been stratified by centrifugation. Centrifugation of living eggs stratifies the organelles yet retains them in the normal cytoplasmic milieu. The local increase in intracellular free Ca2+ in each layer was directly measured under physiological conditions using theta-tubing, double-barreled, Ca2(+)-sensitive microelectrodes in which one barrel was filled with the Ca2+ sensor and the other was filled with Ins(1,4,5)P3 for microinjection. The two tips of these electrodes were very close to each other (3 microns apart) enabling us to measure the kinetics of both the highly localized intracellular Ca2+ release and its subsequent removal in response to Ins(1,4,5)P3 injection. Upon Ins(1,4,5)P3 injection, the ER-enriched layer exhibited the largest release of Ca2+ in a dosage-dependent manner, whereas the other layers, mitochondria, lipid, and yolk, released 10-fold less Ca2+ in a dosage-independent manner. The removal of released Ca2+ took place within approximately 1 min. The sensitivity to Ins(1,4,5)P3 and the time course of intracellular Ca2+ release in the unstratified (unactivated) egg is nearly identical to that observed in the ER layer of the stratified egg. Our data suggest that the ER is the major organelle of the Ins(1,4,5)P3-sensitive Ca2+ store in the egg of Xenopus laevis.