Further Evidence for Inactivation of Fructose-1,6-bisphosphatase at the Beginning of SO2 Fumigation. Increase in Fructose-1,6-bisphosphate and Decrease in Fructose-6-phosphate in SO2-Fumigated Spinach Leaves

The substrate level of the photosynthetic reductive pentosephosphate cycle in spinach leaves during SO₂ fumigation wassurveyed. At the beginning of SO₂ fumigation, fructose-1,6-bisphosphateincreased and fructose-6-phosphate decreased, while ribulose-1,5-bisphosphateremained unchanged and 3-phosphoglyceric acid rapidly decreased.These results suggested that the inhibition of photosynthesisin spinach leaves with SO₂ might be due to inactivation of fructose-1,6-bisphosphatase. (Received May 26, 1982; Accepted September 27, 1982)     

Protein Metabolism in the Domestic Fowl

The metabolic half lives of glycine in the tissue-proteins of the rooster were determined by single oral dose of 2-C¹⁴ glycine before measuring the amount of synthesized glycine in the rooster by ?constant pool? method. The specific activity of glycine originated from the purine ring of uric acid showed the highest value for 5 hrs. after administration, following rapid decrease until 7 days, thereafter slower one.

Although the specific activity of glycine in the tissue protein (serum and liver) decreased exponentially, its trend was not distinct in the pectoral muscle, and in the early period its decrease seemed to be considerably fast (t_1/2 about 6 days).

The specific activities of glycine in the serum protein were always higher than those in the liver protein. The metabolic half livers obtained were as follows. Liver: Faster 2 days, slower 11 days. Serum: faster 2 days, slower 11 days. Pectoral muscle: faster 6 days, slower 30 days. Recovery of C¹⁴ into 4-C and 5-C in the purine ring of excreted uric acid during 24 hours after the administration of isotope was about 24%.     

Studies on cephalopod rhodopsin. Conformational changes in chromophore and protein during the photoregeneration process

The ultraviolet absorbance of squid and octopus rhodopsin changes reversibly at 234 nm and near 280 nm in the interconversion of rhodopsin and metarhodopsin. The absorbance change near 280 nm is ascribed to both protein and chromophore parts. Rhodopsin is photoregenerated from metarhodopsin via an intermediate, P380, on irradiation with yellow light (λ > 520 nm). The ultraviolet absorbance decreases in the change from rhodopsin to metarhodopsin and recovers in two steps; mostly in the process from metarhodopsin to P380 and to a lesser extent in the process from P380 to rhodopsin. P380 has a circular dichroism (CD) band at 380 nm and its magnitude is the same order as that of rhodopsin. Thus it is considered that the molecular structure of P380 is close to that of rhodopsin and that the chromophore is fixed to opsin as in rhodopsin. In the change from metarhodopsin to P380, the chromophore is isomerized from the all-trans to the 11-cis form, and the conformation of opsin changes to fit 11-cis retinal. In the change from P380 to rhodopsin, a small change in the conformation of the protein part and the protonation of the Schiff base, the primary retinal-opsin link, occur.     

Functional development of photosystems I and II in dark-grown pine seedlings

Green plastids prepared from seedlings of Pinus silvestris harvestedafter three weeks of growth in the dark, without exposure tolight, catalyzed photoreductions of methyl viologen and nicotinamide-adeninedinucleotide phosphate, and cyclic photophosphory-lation withN-methylphenazonium methosulfate, but could not catalyze thephotoreduction of 2,4-dichlorophenol indophenol in the absenceand presence of diphenylcarbazide. In dark-grown seedlings ofPinus silvestris, functional photosystem I developed with noexposure to light, but no photosystem II activity was abserved. (Received August 22, 1973; )     

Inhibition of activation of human peripheral blood eosinophils by Y-24180, an antagonist to platelet-activating factor receptor.

We examined the effects of Y-24180, a potent and long-acting antagonist to platelet-activating factor (PAF) receptor, on the PAF- or leukotriene B4 (LTB4)-induced activation of eosinophils using human peripheral blood in vitro. As activation markers, CD11b expression level and soluble intercellular adhesion molecule-1 (sICAM-1)-binding activity were analyzed by flow cytometry. Y-24180 significantly inhibited PAF-induced increase in the ratio of strongly positive cells for CD11b expression and sICAM-1 binding at 0.01 microM or more. WEB 2086, another PAF receptor antagonist, also inhibited the increase significantly at 1 microM or more. LTB4-induced increases in the ratio of strongly positive cells for CD11b expression and sICAM-1 binding were inhibited by Y-24180 at 1 microM, but not WEB 2086 up to 10 microM. These results indicate that Y-24180 inhibits the PAF- or LTB4-induced activation of eosinophils in human peripheral blood more potently than WEB 2086.     

Purification and characterization of fetal bovine serum beta-N-acetyl-D-galactosaminyltransferase and beta-D-glucuronyltransferase involved in chondroitin sulfate biosynthesis.

beta-N-Acetylgalactosaminyltransferase II and beta-glucuronyltransferase II, involved in chondroitin sulfate biosynthesis, transfer an N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcA) residue, respectively, through beta-linkages to an acceptor chondroitin oligosaccharide derived from the repeating disaccharide region of chondroitin sulfate. They were copurified from fetal bovine serum approximately 2500-fold and 850-fold, respectively, by sequential chromatographies on Red A-agarose, phenyl-Sepharose, S-Sepharose and wheat germ agglutinin-agarose. Identical and inseparable chromatographic profiles of both glycosyltransferase activities obtained through the above chromatographic steps and gel filtration suggest that the purified enzyme activities are tightly coupled, which could imply a single enzyme with dual transferase activities; beta-N-acetylgalactosaminyltransferase and beta-glucuronyltransferase, reminiscent of the heparan sulfate polymerase reaction. However, when a polymerization reaction was performed in vitro with the purified serum enzyme preparation under the polymerization conditions recently developed for the chondroitin-synthesizing system, derived from human melanoma cells, each monosaccharide transfer took place, but no polymerization occurred. These results may suggest that the purified serum enzyme preparation contains both beta-N-acetylgalactosaminyltransferase II and beta-glucuronyltransferase II activities on a single polypeptide or on the respective polypeptides forming an enzyme complex, but is different from that obtained from melanoma cells in that it transfers a single GalNAc or GlcA residue but does not polymerize chondroitin.