scholarly journals Modulation of mannosylphosphodolichol synthase and dolichol kinase activity in Trichoderma, related to protein secretion.

1994 ◽  
Vol 41 (3) ◽  
pp. 331-337 ◽  
Author(s):  
J Kruszewska ◽  
C P Kubicek ◽  
G Palamarczyk
Keyword(s):  
Kinase Activity ◽  
Tween 80 ◽  
Protein Glycosylation ◽  
Water Soluble ◽  
Dependent Protein ◽  
Elevated Activity ◽  
The Difference ◽  
C 30 ◽  
Exoprotein Secretion ◽  
Mannosyl Transferase

It has been postulated that exoprotein secretion in Trichoderma is related to their O-glycosylation. In the present paper the involvement of phosphodolichol in this process is described and the key role of mannosylphosphodolichol (MPD) synthase in protein O-mannosylation is discussed. The effect of water soluble phospholipid precursors such as choline and Tween 80, known also to increase secretion of cellulases when added to the medium, on MPD-synthase activity is presented. This effect is positive in the Trichoderma reesei QM 9414 (a low producing strain) but has no influence on the enzyme activity from the RUT C-30 strain selected to overproduce secretion of exoproteins and known to contain an increased cellular amount of endoplasmic reticulum. The positive effect of addition of choline and Tween to the medium on the level of dolichol kinase activity is also demonstrated. The influence of cultivation temperature on the activity of the various enzymes involved in dolichol-dependent protein glycosylation i.e. MPD-synthase, dolichyl kinase and MPD/Protein mannosyl transferase was tested. For all enzymes cultivation at 35 degrees C led to the elevated activity, which was most striking for dolichol kinase, whereas for MPD-synthase and MPD/Protein mannosyl transferase the difference was only apparent in the assay when endogenous phosphodolichol was used as a substrate. Furthermore, lipid extract from the membranes cultivated at elevated temperature, when added to the enzyme obtained from Trichoderma grown at 25 degrees C, enhanced the dolichol kinase activity measured in the absence of exogenous dolichol.(ABSTRACT TRUNCATED AT 250 WORDS)

Molecular Forms of Human Protein C: Comparison and Distribution in Human Adult Plasma

1989 ◽  
Vol 62 (03) ◽  
pp. 902-905 ◽  
Author(s):  
Brian S Greffe ◽  
Marilyn J Manco-Johnson ◽  
Richard A Marlar
Keyword(s):  
Heavy Chain ◽  
Protein C ◽  
Molecular Forms ◽  
Post Translational Modification ◽  
Single Chain ◽  
Beta Form ◽  
Sds Page ◽  
Dependent Protein ◽  
Adult Plasma ◽  
The Difference

SummaryProtein C (PC) is a vitamin K-dependent protein which functions as both an anticoagulant and profibrinolytic. It is synthesized as a single chain protein (SC-PC) and post-transla-tionally modified into a two chain form (2C-PC). Two chain PC consists of a light chain (LC) and a heavy chain (HC). The present study was undertaken to determine the composition of the molecular forms of PC in plasma. PC was immunoprecipitated, subjected to SDS-PAGE and Western blotting. The blots were scanned by densitometry to determine the distribution of the various forms. The percentage of SC-PC and 2C-PC was found to be 10% and 90% respectively. This is in agreement with previous work. SC-PC and the heavy chain of 2C-PC consisted of three molecular forms (“alpha”, “beta”, and “gamma”). The “alpha” form of HC is the standard 2C form with a MW of 40 Kd. The “beta” form of HC has also been described and has MW which is 4 Kd less than the “alpha” form. The “gamma” species of the SC and 2C-PC has not been previously described. However, its 3 Kd difference from the “beta” form could be due to modification of the “beta” species or to a separate modification of the alpha-HC. The LC of PC was shown to exist in two forms (termed form 1 and form 2). The difference between these two forms is unknown. The molecular forms of PC are most likely due to a post-translational modification (either loss of a carbohydrate or a peptide) rather than from plasma derived degradation.

ANALISA KANDUNGAN BETA-GLUKAN LARUT AIR DAN LARUT ALKALI DARI TUBUH BUAH JAMUR TIRAM (Pleurotus ostreatus) DAN SHIITAKE (Lentinus edodes)

2013 ◽  
Vol 13 (3) ◽  
Author(s):  
Netty Widyastuti ◽  
Teguh Baruji ◽  
Henky Isnawan ◽  
Priyo Wahyudi ◽  
Donowati Donowati
Keyword(s):  
Molecular Structure ◽  
Molecular Weight ◽  
Immune System ◽  
Pleurotus Ostreatus ◽  
Water Soluble ◽  
Low Molecular Weight ◽  
Lentinus Edodes ◽  
Beta Glucan ◽  
Oyster Mushrooms ◽  
The Difference

Beta glucan is a polysaccharide compound, generally not soluble inwater and resistant to acid. Beta glucan is used as an immunomodulator (enhancing the immune system) in mammals is usually a beta-glucan soluble in water, easily absorbed and has a low molecular weight. Several example of beta-glucan such as cellulose (β-1 ,4-glucan), lentinan (β-1 0.6-glucan) and (β-1 ,3-glucan), pleuran (β-1, 6 and β-1 ,3-glucan) are isolated from species of fungi Basidiomycota include mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes).The purpose of thisresearch activity is to obtain beta-glucan compound that can be dissolved in water and in alkali derived from fungi Basidiomycota, i.e, Oyster mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes). The result of beta-glucan compared to characterize the resulting beta glucan that is molecular structure . The difference of beta glucan extraction is based on the differences in solubility of beta-glucan. Beta glucan could be water soluble and insoluble water.

scholarly journals Pho85p, a cyclin-dependent protein kinase, and the Snf1p protein kinase act antagonistically to control glycogen accumulation in Saccharomyces cerevisiae.

1996 ◽  
Vol 16 (8) ◽  
pp. 4357-4365 ◽  
Author(s):  
D Huang ◽  
I Farkas ◽  
P J Roach
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Mutant Gene ◽  
Glycogen Synthase Kinase ◽  
Partial Purification ◽  
Glycogen Accumulation ◽  
Dependent Protein

In Saccharomyces cerevisiae, nutrient levels control multiple cellular processes. Cells lacking the SNF1 gene cannot express glucose-repressible genes and do not accumulate the storage polysaccharide glycogen. The impaired glycogen synthesis is due to maintenance of glycogen synthase in a hyperphosphorylated, inactive state. In a screen for second site suppressors of the glycogen storage defect of snf1 cells, we identified a mutant gene that restored glycogen accumulation and which was allelic with PHO85, which encodes a member of the cyclin-dependent kinase family. In cells with disrupted PHO85 genes, we observed hyperaccumulation of glycogen, activation of glycogen synthase, and impaired glycogen synthase kinase activity. In snf1 cells, glycogen synthase kinase activity was elevated. Partial purification of glycogen synthase kinase activity from yeast extracts resulted in the separation of two fractions by phenyl-Sepharose chromatography, both of which phosphorylated and inactivated glycogen synthase. The activity of one of these, GPK2, was inhibited by olomoucine, which potently inhibits cyclin-dependent protein kinases, and contained an approximately 36-kDa species that reacted with antibodies to Pho85p. Analysis of Ser-to-Ala mutations at the three potential Gsy2p phosphorylation sites in pho85 cells implicated Ser-654 and/or Thr-667 in PHO85 control of glycogen synthase. We propose that Pho85p is a physiological glycogen synthase kinase, possibly acting downstream of Snf1p.

Tenellones A and B from aDiaporthesp.:  Two Highly Substituted Benzophenone Inhibitors of Parasite cGMP-Dependent Protein Kinase Activity

2005 ◽  
Vol 68 (4) ◽  
pp. 611-613 ◽  
Author(s):  
Chaowei Zhang ◽  
John G. Ondeyka ◽  
Kithsiri B. Herath ◽  
Ziqiang Guan ◽  
Javier Collado ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Dependent Protein

Analytical subcellular distribution of cAMP-dependent protein kinase activity in bull sperm

1984 ◽  
Vol 10 (4) ◽  
pp. 433-444 ◽  
Author(s):  
Claude C. Pariset ◽  
Jacqueline S. Weinman ◽  
Francoise T. Escaig ◽  
Michele Y. Guyot ◽  
Francine C. Iftode ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Subcellular Distribution ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Bull Sperm
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