A minor, protein-containing galactomannan from a sodium carbonate extract of Cordyceps sinensis

1986 ◽  
Vol 156 ◽  
pp. 189-197 ◽  
Author(s):  
Tadashi Kiho ◽  
Hajime Tabata ◽  
Shigeo Ukai ◽  
Chihiro Hara
Keyword(s):  
Sodium Carbonate ◽  
Cordyceps Sinensis ◽  
Minor Protein ◽  
A Minor

Functional specificity of jejunal brush-border pteroylpolyglutamate hydrolase in pig

1991 ◽  
Vol 260 (6) ◽  
pp. G865-G872 ◽  
Author(s):  
C. J. Chandler ◽  
D. A. Harrison ◽  
C. A. Buffington ◽  
N. A. Santiago ◽  
C. H. Halsted
Keyword(s):  
Brush Border ◽  
Protein Band ◽  
Major Protein ◽  
Functional Specificity ◽  
Major Protein Band ◽  
Regional Location ◽  
Minor Protein ◽  
A Minor ◽  
Hydrolysis Of

To determine the functional specificity of intestinal brush-border pteroylpolyglutamate hydrolase (PPH), we compared the regional location of in vivo hydrolysis of pteroyltriglutamate (PteGlu3) with the location of activity and immunoreactivity of the enzyme in the pig. After in vivo incubations, PteGlu3 hydrolytic products were recovered from intestinal segments in the jejunum but not from the ileum. Brush-border PPH activity in fractionated mucosa was 10-fold greater in the jejunum than in the ileum, whereas the activity of intracellular PPH was increased in the distal ileum. Antibodies to purified brush-border PPH identified a major protein band at 120 kDa and a minor protein band at 195 kDa in solubilized jejunal brush border. Immunohistochemistry identified the enzyme only on the brush-border surface of the jejunum, whereas an immunoblot of solubilized brush-border membranes identified brush-border PPH in the jejunum but not in the ileum. The parallel of the regional location of in vivo hydrolysis of PteGlu3 with the location of brush-border PPH activity and immunoreactivity demonstrates the functional specificity of this enzyme in folate digestion.

Oxidative cyclization of carbonyl derivatives. 5-Imino-Δ1-1,2,4-triazolines from alkylideneimino guanidines

1978 ◽  
Vol 56 (16) ◽  
pp. 2194-2196 ◽  
Author(s):  
Lubomira M. Cabelkova-Taguchi ◽  
John Warkentin
Keyword(s):  
Sodium Carbonate ◽  
Oxidation Product ◽  
Methylene Chloride ◽  
Oxidative Cyclization ◽  
Lead Tetraacetate ◽  
Carbonyl Derivatives ◽  
A Minor ◽  
Major Oxidation

Treatment of 2-propylideneimino guanidinium acetate with lead tetraacetate, in methylene chloride containing solid sodium carbonate, afforded the previously unknown 3,3-dimethyl-5-imino-Δ1-1,2,4-triazoline. Similarly, N,N′-diphenyl-N″-(2-propylideneimino)guanidinium acetate afforded Z-4-phenyl-5-phenylimino-Δ1-1,2,4-triazoline as the major oxidation product and the corresponding E isomer as a minor product. Stereochemistry was established spectrophotometrically and also by isomerizing the minor (E) isomer to the major (Z) isomer.

scholarly journals Alteration in Molecular Structure of Alkali Activated Slag with Various Water To Binder Ratios Under Accelerated Carbonation

2021 ◽  
Author(s):  
Thi Nhan Nguyen ◽  
Quoc Phung ◽  
Ziyou Yu ◽  
Lander Frederickx ◽  
Diederik Jacques ◽  
...  
Keyword(s):  
Sodium Carbonate ◽  
Cementitious Materials ◽  
Mas Nmr ◽  
Accelerated Carbonation ◽  
Alkali Activated Slag ◽  
Before And After ◽  
Activated Slag ◽  
A Charge ◽  
A Minor ◽  
Alkali Activated

Abstract Carbonation of alkali activated materials is one of the main deteriorations affecting their durability. However, current understanding in structural alteration of these materials exposed to an environment inducing carbonation at nano/micro scale remains limited. This study examined the evolution of phase assemblages of alkali activated slag mortars subjected to accelerated carbonation (1% CO2, 60% relative humidity, up to 28 day carbonation) using XRD, FTIR and 29Si, 27Al, 23Na MAS NMR. Samples with three water to binder (w/b) ratios (0.35, 0.45, and 0.55) were investigated. The results show that the phase assemblages mainly consisted of C-A-S-H, disordered remnant aluminosilicate binder, and a minor hydrotalcite as a secondary product. Upon carbonation, calcium carbonate is mainly formed as the vaterite polymorph, while no sodium carbonate is found after carbonation as commonly reported. The sodium acts primarily as a charge balancing ion without producing sodium carbonate as a final carbonation product in 28-day carbonated materials. The C-A-S-H structure becomes more cross-linked due to the decalcification of this phase evidenced by the appearance of Q4 groups, which replace the Q1 and Q2 ones as observed in the 29Si MAS NMR spectra, and the dominance of Al (IV) in 27Al MAS NMR. Especially, unlike cementitious materials, the influence of w/b ratio on the crystalline phase formation and structure of C-A-S-H in the alkali activated mortars before and after carbonation is limited.

H protein, a minor protein of TMV virions, containssequences of the viral coat protein

Virology ◽  
1983 ◽  
Vol 126 (2) ◽  
pp. 429-448 ◽  
Author(s):  
Candace Whitmer Collmer ◽  
Volker M. Vogt ◽  
Milton Zaitlin
Keyword(s):  
Coat Protein ◽  
Protein A ◽  
Viral Coat Protein ◽  
Minor Protein ◽  
Viral Coat ◽  
A Minor ◽  
H Protein

scholarly journals Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin.

1984 ◽  
Vol 160 (3) ◽  
pp. 788-798 ◽  
Author(s):  
M E Perkins
Keyword(s):  
Specific Binding ◽  
Surface Proteins ◽  
Malarial Parasite ◽  
Ligand Molecule ◽  
Glycophorin A ◽  
Surface Coat ◽  
Receptor Proteins ◽  
Erythrocyte Surface ◽  
Minor Protein ◽  
A Minor

Invasion of erythrocytes by the malarial parasite is a receptor-mediated process. P. falciparum merozoites recognize and bind to erythrocyte surface sialoglycoproteins, glycophorins A and B, and the glycophorins bind to saturable sites on the merozoite surface. The purpose of the present work was to identify a receptor or ligand molecule on the merozoite surface that mediates binding to the erythrocyte. A fraction containing the sialoglycoproteins was coupled to an acrylamide matrix and incubated with metabolically labeled merozoites. A merozoite protein of 155 kD that labeled prominently with [3H]glycine bound to glycophorin. A minor protein of 130 kD also bound. Both proteins are rich in proline and glycine, poor in methionine, and may be related. The proteins are also stable to heating to 100 degrees C for 10 min. Immunoelectron microscopy demonstrated that the 155 kD and 130 kD proteins are located on the merozoite surface coat. The antibodies significantly inhibited merozoite invasion into erythrocytes and also binding of the proteins to the glycophorin-matrix. The specific binding of the 155-kD and 130-kD proteins to the erythrocyte receptor and the demonstration that they are located on the merozoite surface suggest they could be receptor proteins that mediate binding of the merozoite to the erythrocyte surface.

scholarly journals Vault Poly(ADP-Ribose) Polymerase Is Associated with Mammalian Telomerase and Is Dispensable for Telomerase Function and Vault Structure In Vivo

2004 ◽  
Vol 24 (12) ◽  
pp. 5314-5323 ◽  
Author(s):  
Yie Liu ◽  
Bryan E. Snow ◽  
Valerie A. Kickhoefer ◽  
Natalie Erdmann ◽  
Wen Zhou ◽  
...  
Keyword(s):  
Telomere Length ◽  
Telomerase Activity ◽  
Molecular Assembly ◽  
Cellular Functions ◽  
Telomere Function ◽  
Minor Protein ◽  
The Stability ◽  
A Minor

ABSTRACT Vault poly(ADP-ribose) polymerase (VPARP) was originally identified as a minor protein component of the vault ribonucleoprotein particle, which may be involved in molecular assembly or subcellular transport. In addition to the association of VPARP with the cytoplasmic vault particle, subpopulations of VPARP localize to the nucleus and the mitotic spindle, indicating that VPARP may have other cellular functions. We found that VPARP was associated with telomerase activity and interacted with exogenously expressed telomerase-associated protein 1 (TEP1) in human cells. To study the possible role of VPARP in telomerase and vault complexes in vivo, mVparp-deficient mice were generated. Mice deficient in mVparp were viable and fertile for up to five generations, with no apparent changes in telomerase activity or telomere length. Vaults purified from mVparp-deficient mouse liver appeared intact, and no defect in association with other vault components was observed. Mice deficient in mTep1, whose disruption alone does not affect telomere function but does affect the stability of vault RNA, showed no additional telomerase or telomere-related phenotypes when the mTep1 deficiency was combined with an mVparp deficiency. These data suggest that murine mTep1 and mVparp, alone or in combination, are dispensable for normal development, telomerase catalysis, telomere length maintenance, and vault structure in vivo.

scholarly journals Purification of the phosphorylated night form and dephosphorylated day form of phosphoenolpyruvate carboxylase from Bryophyllum fedtschenkoi

1986 ◽  
Vol 239 (1) ◽  
pp. 213-220 ◽  
Author(s):  
G A Nimmo ◽  
H G Nimmo ◽  
I D Hamilton ◽  
C A Fewson ◽  
M B Wilkins
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Enzyme Concentration ◽  
Amino Acid Sequences ◽  
Major Protein ◽  
Protein Subunit ◽  
Minor Protein ◽  
Low Sensitivity ◽  
A Minor ◽  
Related Amino Acid

Phosphoenolpyruvate carboxylase of Bryophyllum fedtschenkoi was shown to exist in two forms: a night form, which is phosphorylated and has low sensitivity to inhibition by malate, and a day form, which is dephosphorylated and 10 times more sensitive to malate. The day and night forms of the enzyme were purified retaining their distinct malate sensitivities and phosphorylation states. The purified enzymes contained a major protein (subunit Mr 112,000) and a minor protein (subunit Mr 123,000). The two polypeptides appeared to have closely related amino acid sequences and were present in a similar ratio in extracts that had been prepared rapidly. The phosphate present in the night form of the enzyme was covalently bound to serine. It was not a catalytic intermediate. Alkaline phosphatase removed the phosphate group in vitro and increased the malate sensitivity of the enzyme to that observed for the day form. Both the day and night forms of the enzyme were probably tetramers, and their apparent Mr was lowered by the presence of malate, but was unaffected by Mg2+ ions, EDTA, a rise in pH or a 10-fold change in enzyme concentration. The rapid loss of malate sensitivity, observed in extracts of leaves prepared during the day and at night, was shown to be due to proteolysis of the enzyme. It was slowed in the presence of malate and by phosphorylation of the enzyme.

scholarly journals Characterization of Colicin S4 and Its Receptor, OmpW, a Minor Protein of the Escherichia coli Outer Membrane

1999 ◽  
Vol 181 (11) ◽  
pp. 3578-3581 ◽  
Author(s):  
Holger Pilsl ◽  
David Smajs ◽  
Volkmar Braun
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Receptor Binding ◽  
Terminal Region ◽  
Receptor Binding Domain ◽  
Immunity Protein ◽  
Minor Protein ◽  
A Minor ◽  
Sequence Similarities

ABSTRACT Analysis of the nucleotide sequence of an Escherichia coli colicin S4 determinant revealed 76% identity to the pore-forming domain of the colicin A protein, 77% identity to the colicin A immunity protein, and 82% identity to the colicin A lysis protein. The N-terminal region, which is responsible for the Tol-dependent uptake of colicin S4, has 94% identity to the N-terminal region of colicin K. By contrast, the predicted receptor binding domain shows no sequence similarities to other colicins. Mutants that lacked the OmpW protein were resistant to colicin S4.

scholarly journals Hydrolysis of fucosyl-GM1 ganglioside by purified pellet-associated human brain and human liver α-l-fucosidases without activator proteins or detergents

1990 ◽  
Vol 266 (2) ◽  
pp. 491-496 ◽  
Author(s):  
R L Hopfer ◽  
S W Johnson ◽  
M Masserini ◽  
A Giuliani ◽  
J A Alhadeff
Keyword(s):  
Human Brain ◽  
Specific Activity ◽  
Protein Band ◽  
Enzymic Activity ◽  
Gm1 Ganglioside ◽  
Ph Optimum ◽  
Activator Proteins ◽  
Minor Protein ◽  
A Minor ◽  
Triton X

Pellet-associated human brain alpha-L-fucosidase was solubilized with 0.5% (w/v) Triton X-100 and purified by affinity chromatography on agarose-6-aminohexanoyl-fucosamine resin. The procedure resulted in a 290,000-fold purification, a 58% yield and a final specific activity of 11,500 nmol/min per mg of protein. Isoelectric focusing indicated that all six major isoforms (with pI values between 4.1 and 5.3) present in crude brain pellet preparations were purified by the affinity technique. SDS/PAGE indicated the presence of one subunit (54 kDa) and a minor protein band at 67 kDa, which presumably is a contaminant since it was not immunoreactive on Western blotting. The pH optimum of the brain enzyme and its apparent Km for the synthetic substrate 4-methylumbelliferyl alpha-L-fucopyranoside were 5.5 and 0.07 mM respectively. Pellet-associated human brain and liver alpha-L-fucosidases were both capable of hydrolysing fucosyl-GM1 ganglioside without activator proteins or detergents. Linear hydrolysis rates were found only for short incubation times (1-5 min). Optimal enzymic activity at 37 degrees C was found at pH 3.4 for both alpha-L-fucosidases, with no activity at pH values above 4.0.

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