scholarly journals Identification and characterization of a phospholipase C activity in resident mouse peritoneal macrophages. Inhibition of the enzyme by phenothiazines

1981 ◽  
Vol 197 (2) ◽  
pp. 523-526 ◽  
Author(s):  
Paul D. Wightman ◽  
Mary Ellen Dahlgren ◽  
James C. Hall ◽  
Philip Davies ◽  
Robert J. Bonney
Keyword(s):  
Phospholipase C ◽  
High Activity ◽  
Peritoneal Macrophages ◽  
Ph Optimum ◽  
Reaction Velocity ◽  
Neutral Ph ◽  
Maximum Reaction ◽  
Mouse Peritoneal Macrophages ◽  
Identification And Characterization

Resident mouse peritoneal macrophages contain a phospholipase C of high activity that is specific for phosphatidylinositol. The activity has a neutral pH optimum, is Ca2+-dependent and has a maximum reaction velocity of 525nmol/h per mg of protein. Certain phenothiazines are potent inhibitors of this activity.

Soluble neutral maltase–glucoamylase from the small intestine: separation and characterization of components with differing affinity for concanavalin A

1982 ◽  
Vol 60 (11) ◽  
pp. 1007-1013 ◽  
Author(s):  
G. Forstner ◽  
A. Salvatore ◽  
L. Lee ◽  
J. Forstner
Keyword(s):  
Concanavalin A ◽  
Gradient Elution ◽  
Soluble Form ◽  
Rat Intestine ◽  
Ph Optimum ◽  
Molecular Weights ◽  
Neutral Ph ◽  
Membrane Bound ◽  
Sepharose 4B

Intestinal maltase with a neutral pH optimum exists in both a brush border membrane-bound form and a soluble form in suckling rat intestine. Previous experiments in our laboratory have shown that the soluble enzyme contains a component which binds much more tightly to concanavalin A (ConA) than solubilized forms of the membrane enzyme. We studied the origin of this component by subjecting neutral, soluble maltase activity to chromatography on Sepharose 4B at age 13, 18 (preweaning), and 25 (postweaning) days. At 13 days, two maltase peaks were obtained with approximate molecular weights of 400 000 (peak I) and 150 000 (peak II). Peak II was less prominent at 18 days and was absent at 25 days. At 13 days, the majority of peak I consisted of material which was bound between 0.025 and 0.05 M α-methyl mannoside on gradient elution chromatography of ConA-Sepharose. Peak II contained material which eluted between 0.075 and 0.3 M α-methyl mannoside. At 25 days, all of the soluble maltase eluted between 0.025 and 0.04 M α-methyl mannoside. Peak I and peak II maltases had similar pH optima and Km's for maltase. Peak II maltase had a fourfold greater activity toward glycogen than peak I maltase with approximately the same activity for palatinose, turanose, and trehalose. Both maltases were precipitated by an antibody raised against adult membrane-bound maltase. Soluble maltase with neutral pH activity in the suckling rat intestine, therefore, consists of two immunologically related isozymes which differ in their molecular weight, their binding by ConA, and their specificity for glycogen. The small isozyme disappears at or about the time of weaning.

scholarly journals Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1224-1228 ◽  
Author(s):  
S Rajagopalan ◽  
SV Pizzo
Keyword(s):  
Degradation Products ◽  
Peritoneal Macrophages ◽  
Receptor System ◽  
Human Fibrinogen ◽  
Murine Peritoneal Macrophage ◽  
High Affinity ◽  
Macrophage Receptors ◽  
Low Concentrations ◽  
Mouse Peritoneal Macrophages

Abstract The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.

Characterization of membrane melatonin receptor in mouse peritoneal macrophages: inhibition of adenylyl cyclase by a pertussis toxin-sensitive G protein

1999 ◽  
Vol 95 (1-2) ◽  
pp. 85-94 ◽  
Author(s):  
Antonio Garcı́a-Pergañeda ◽  
Juan M Guerrero ◽  
Mohammed Rafii-El-Idrissi ◽  
M Paz Romero ◽  
David Pozo ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
G Protein ◽  
Pertussis Toxin ◽  
Peritoneal Macrophages ◽  
Melatonin Receptor ◽  
Mouse Peritoneal Macrophages

scholarly journals Characterization of deoxyribonuclease activities derived from control and inflammation-associated mouse peritoneal macrophages

1984 ◽  
Vol 220 (2) ◽  
pp. 561-568
Author(s):  
G E Brown ◽  
T P Karpetsky ◽  
K Rictor ◽  
A Rahman
Keyword(s):  
Peritoneal Cavity ◽  
Peripheral Blood ◽  
Peritoneal Macrophages ◽  
Apparent Size ◽  
Blood Components ◽  
Cell Type ◽  
Specific Subset ◽  
Mouse Peritoneal Macrophages ◽  
Increased Activity

Native DNAase (deoxyribonuclease) activities derived from mouse peritoneal cavity and peripheral blood components were separated, detected, and characterized by electrophoresis into polyacrylamide gels containing DNA, followed by incubation of the gels, and staining of the substrate to reveal only the DNAase activities. Resident peritoneal macrophages contained 12 DNAase-II-like activities that were characteristic of that cell type, whereas lymphocytes and granulocytes each contained five DNAases. Induction of inflammation by peritoneal injection of thioglycollate resulted in changes in macrophage DNAase expression, including: increased total DNAase activity, a decrease in the number of activities from 12 to 11, increased activity of a specific subset of the enzymes, and a change in the apparent size of a specific subset of the enzymes. Electrophoretic and enzymic properties and sensitivity to endo-beta-N-acetylglucosaminidase H indicated that the macrophage activities probably represented charge variants of one or two parent peptide chains.

scholarly journals Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1224-1228 ◽  
Author(s):  
S Rajagopalan ◽  
SV Pizzo
Keyword(s):  
Degradation Products ◽  
Peritoneal Macrophages ◽  
Receptor System ◽  
Human Fibrinogen ◽  
Murine Peritoneal Macrophage ◽  
High Affinity ◽  
Macrophage Receptors ◽  
Low Concentrations ◽  
Mouse Peritoneal Macrophages

The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.

MICROBIAL BETA-GALACTOSIDASE: A SURVEY FOR NEUTRAL pH OPTIMUM ENZYMES

1974 ◽  
Vol 37 (4) ◽  
pp. 199-202 ◽  
Author(s):  
L. C. Blankenship ◽  
P. A. Wells
Keyword(s):  
Ammonium Sulfate ◽  
Dairy Products ◽  
Skim Milk ◽  
Product Inhibition ◽  
Ph Optimum ◽  
Neutral Ph ◽  
Cation Activation ◽  
Pure Cultures ◽  
Beta Galactosidase

Pure cultures of yeast, molds, and bacteria were screened for neutral pH optimum β-galactosidases (lactases) that would be suitable in dairy products applications. Only 2 of 125 identified and 10 of 250 unidentified cultures warranted further study. These cultures produced high levels of β-galactosidase with moderate galactose product inhibition. Characterization of the partially purified enzymes from unidentified cultures revealed that all required either Na+, K+ or Mg++ cation activation, were inhibited by Cu+ +, Mn+ +, and Fe+ + +, were most active around pH 6.8, and were unstable during storage (at either – 196 C or 4 C) except in the presence of 0.5 m ammonium sulfate. Most of the enzymes compared favorably in performance with a commercially available β-galactosidase when tested in skim milk.

Identification and Characterization of a New Phospholipase C-like Protein, PLC-L2

1999 ◽  
Vol 266 (1) ◽  
pp. 97-103 ◽  
Author(s):  
Makiko Otsuki ◽  
Kiyoko Fukami ◽  
Takashi Kohno ◽  
Jun Yokota ◽  
Tadaomi Takenawa
Keyword(s):  
Phospholipase C ◽  
Identification And Characterization
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