Studies on Streptomyces scabies II. Stimulation of Melanin Production by Amino Acids

1954 ◽  
Vol 81 (2) ◽  
pp. 98 ◽  
Author(s):  
John P. Hollis
Keyword(s):  
Amino Acids ◽  
Streptomyces Scabies ◽  
Melanin Production ◽  
Stimulation Of

Cloning, characterization, and gene organization of K-Cl cotransporter from pig and human kidney and C. elegans

1998 ◽  
Vol 275 (4) ◽  
pp. F550-F564 ◽  
Author(s):  
Eli J. Holtzman ◽  
Sumit Kumar ◽  
Carol A. Faaland ◽  
Fern Warner ◽  
Paul J. Logue ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Kidney ◽  
Gene Organization ◽  
Kidney Cells ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
C Elegans ◽  
Transmembrane Segments ◽  
Extracellular Loops ◽  
Stimulation Of

We isolated and characterized the cDNAs for the human, pig, and Caenorhabditis elegansK-Cl cotransporters. The pig and human homologs are 94% identical and contain 1,085 and 1,086 amino acids, respectively. The deduced protein of the C. elegans K-Cl cotransporter clone (CE-KCC1) contains 1,003 amino acids. The mammalian K-Cl cotransporters share ∼45% similarity with CE-KCC1. Hydropathy analyses of the three clones indicate typical KCC topology patterns with 12 transmembrane segments, large extracellular loops between transmembrane domains 5 and 6 (unique to KCC), and large COOH-terminal domains. Human KCC1 is widely expressed among various tissues. This KCC1 gene spans 23 kb and is organized in 24 exons, whereas the CE-KCC1 gene spans 3.5 kb and contains 10 exons. Transiently and stably transfected human embryonic kidney cells (HEK-293) expressing the human, pig, and C. elegans K-Cl cotransporter fulfilled two (pig) or five (human and C. elegans) criteria for increased expression of the K-Cl cotransporter. The criteria employed were basal K-Cl cotransport; stimulation of cotransport by swelling, N-ethylmaleimide, staurosporine, and reduced cell Mg concentration; and secondary stimulation of Na-K-Cl cotransport.

scholarly journals Stimulation of NSF ATPase Activity by α-SNAP Is Required for SNARE Complex Disassembly and Exocytosis

1997 ◽  
Vol 139 (4) ◽  
pp. 875-883 ◽  
Author(s):  
Richard J.O. Barnard ◽  
Alan Morgan ◽  
Robert D. Burgoyne
Keyword(s):  
Amino Acids ◽  
Atpase Activity ◽  
Binding Sites ◽  
Chromaffin Cells ◽  
Secretory Pathway ◽  
Snare Complex ◽  
Vesicular Traffic ◽  
Protein Dissociation ◽  
Terminal Amino ◽  
Stimulation Of

N-ethylmaleimide–sensitive fusion protein (NSF) and α-SNAP play key roles in vesicular traffic through the secretory pathway. In this study, NH2- and COOH-terminal truncation mutants of α-SNAP were assayed for ability to bind NSF and stimulate its ATPase activity. Deletion of up to 160 NH2-terminal amino acids had little effect on the ability of α-SNAP to stimulate the ATPase activity of NSF. However, deletion of as few as 10 COOH-terminal amino acids resulted in a marked decrease. Both NH2-terminal (1–160) and COOH-terminal (160–295) fragments of α-SNAP were able to bind to NSF, suggesting that α-SNAP contains distinct NH2- and COOH-terminal binding sites for NSF. Sequence alignment of known SNAPs revealed only leucine 294 to be conserved in the final 10 amino acids of α-SNAP. Mutation of leucine 294 to alanine (α-SNAP(L294A)) resulted in a decrease in the ability to stimulate NSF ATPase activity but had no effect on the ability of this mutant to bind NSF. α-SNAP (1–285) and α-SNAP (L294A) were unable to stimulate Ca2+-dependent exocytosis in permeabilized chromaffin cells. In addition, α-SNAP (1–285), and α-SNAP (L294A) were able to inhibit the stimulation of exocytosis by exogenous α-SNAP. α-SNAP, α-SNAP (1–285), and α-SNAP (L294A) were all able to become incorporated into a 20S complex and recruit NSF. In the presence of MgATP, α-SNAP (1–285) and α-SNAP (L294A) were unable to fully disassemble the 20S complex and did not allow vesicle-associated membrane protein dissociation to any greater level than seen in control incubations. These findings imply that α-SNAP stimulation of NSF ATPase activity may be required for 20S complex disassembly and for the α-SNAP stimulation of exocytosis.

Control of mouth opening and pharynx protrusion during feeding in the sea anemone Calliactis parasitica

1975 ◽  
Vol 63 (3) ◽  
pp. 615-626
Author(s):  
I. D. McFarlane
Keyword(s):  
Amino Acids ◽  
Electrical Stimulation ◽  
Reduced Glutathione ◽  
Mouth Opening ◽  
Pulse Frequency ◽  
Sea Anemone ◽  
Conducting System ◽  
Nerve Net ◽  
Calliactis Parasitica ◽  
Stimulation Of

1. Activity in all three known conducting systems (the nerve net, SS1, and SS2) may accompany feeding in Calliactis. The most marked response is an increase in pulse frequency in the SS2 (the endodermal slow conducting system) during mouth opening and pharynx protrusion. 2. Electrical stimulation of the SS2 at a frequency of one shock every 5 s elicits mouth opening and pharynx protrusion in the absence of food. 3. A rise in SS2 pulse frequency is also evoked by food extracts, some amino acids, and in particular by the tripeptide reduced glutathione, which produces a response at a concentration of 10(−5) M. 4. Although the SS2 is an endodermal system, the receptors involved in the response to food appear to be ectodermal. 5. The epithelium that lines the pharynx conducts SS1 pulses, but there is some evidence for polarization of conduction.

scholarly journals EFFECT OF BIOLOGICALLY ACTIVE SUBSTANCES FORMED BY BACCILUS COAGULANS TI ON THE GROWTH OF CROPS

2013 ◽  
Vol 17 (2) ◽  
pp. 53-60
Author(s):  
Tatiana Lisitskaya ◽  
Tatiana Trosheva
Keyword(s):  
Amino Acids ◽  
Plant Biomass ◽  
Bacillus Coagulans ◽  
Biologically Active Substances ◽  
Biologically Active ◽  
Submerged Cultivation ◽  
Peptone Medium ◽  
Active Substances ◽  
Stimulation Of

Abstract The influence of cultural liquid of bacteria, Bacillus coagulans TI on the growth of several crops are studded. It was established that during the submerged cultivation on glucose-peptone medium these bacteria form gibberellins and amino acids. Pre-sowing treatment of seeds with diluted cultural liquid causes the stimulation of plants growth and improves the quality of plant biomass.

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