An extreme halophilic xylanase from camel rumen metagenome with elevated catalytic activity in high salt concentrations

Δ9-Desaturase is a key enzyme in the synthesis of desaturated fatty acyl-CoAs. Desaturase is an integral membrane protein induced in the endoplasmic reticulum by dietary manipulations and then rapidly degraded. The proteolytic machinery that specifically degrades desaturase and other short-lived proteins in the endoplasmic reticulum has not been identified. As the first step in identifying cellular factors involved in the degradation of desaturase, liver subcellular fractions of rats that had undergone induction of this enzyme were examined. In livers from induced animals, desaturase was present in the microsomal, nuclear (P-1), and subcellular fractions (P-2). Incubation of desaturase containing fractions at physiological pH and temperature led to the complete disappearance of the enzyme. Washing microsomes with a buffer containing high salt decreased desaturase degradation activity. N-terminal sequence analysis of desaturase freshly isolated from the P-1 fraction without incubation indicated the absence of three residues from the N terminus, but the mobility of this desaturase preparation on SDS-PAGE was identical to the microsomal desaturase, which contains a masked N terminus under similar purification procedures. Addition of concentrated cytosol or the high-salt wash fraction did not enhance the desaturase degradation in the washed microsomes. Extensive degradation of desaturase in the high-salt washed microsomes could be restored by supplementation of the membranes with the lipid and protein components essential for the reconstituted desaturase catalytic activity. Lysosomotrophic agents leupeptin and pepstatin A were ineffective in inhibiting desaturase degradation. The calpain inhibitor, N-acetyl-leucyl-leucyl-methional, or the proteosome inhibitor, Streptomyces metabolite, lactacystin, did not inhibit the degradation of desaturase in the microsomal or the P-1 and P-2 fractions. These results show that the selective degradation of desaturase is likely to be independent of the lysosomal and the proteosome systems. The reconstitution of complete degradation of desaturase in the high-salt–washed microsomes by the components essential for its catalytic activity reflects that the degradation of this enzyme may depend on a specific orientation of desaturase and intramembranous interactions between desaturase and the responsible protease.

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High resolution electron microscopy of lanthanum phosphate crystals

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100108519 ◽

1978 ◽

Vol 36 (1) ◽

pp. 274-275

Author(s):

J. C. Wheatley ◽

J. M. Cowley

Keyword(s):

Electron Microscopy ◽

Catalytic Activity ◽

High Resolution ◽

Petroleum Industry ◽

High Resolution Electron Microscopy ◽

Lanthanum Phosphate ◽

Good Catalyst ◽

Resolution Electron ◽

Good Catalytic Activity ◽

Physical And Chemical

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).

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The design and catalytic performance of molybdenum active sites on an MCM-41 framework for the aerobic oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran

Catalysis Science & Technology ◽

10.1039/c8cy02291g ◽

2019 ◽

Vol 9 (3) ◽

pp. 811-821 ◽

Cited By ~ 7

Author(s):

Zhao-Meng Wang ◽

Li-Juan Liu ◽

Bo Xiang ◽

Yue Wang ◽

Ya-Jing Lyu ◽

...

Keyword(s):

Catalytic Activity ◽

Active Sites ◽

Aerobic Oxidation ◽

Catalytic Performance ◽

Mcm 41

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.

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Dissolution of α-Iron (Hydr)oxides by Trihydroxamate and Catecholate Siderophores and Oxalate Ligands at High Salt Concentrations and pH 3-6

Environmental Science & Technology ◽

10.1021/es048751e ◽

1967 ◽

Vol 0 (0) ◽

pp. 0-0

Author(s):

J. Cervini-Silva ◽

G. Sposito

Keyword(s):

High Salt

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Prolonged Expression of Procoagulant Activity of Human Platelets Degranulated by Thrombin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649855 ◽

1995 ◽

Vol 74 (03) ◽

pp. 958-961 ◽

Cited By ~ 6

Author(s):

Raelene L Kinlough-Rathbone ◽

Dennis W Perry

Keyword(s):

Catalytic Activity ◽

Thrombus Formation ◽

Annexin V ◽

Human Platelets ◽

Procoagulant Activity ◽

Prothrombinase Complex ◽

Arterial Thrombus ◽

Flowing Blood

SummaryPlatelets are exposed to thrombin when they take part in arterial thrombus formation, and they may return to the circulation when they are freed by fibrinolysis and dislodged by flowing blood. Thrombin causes the expression of procoagulant activity on platelets, and if this activity persists, the recirculating platelets may contribute to subsequent thrombosis. We have developed techniques to degranulate human platelets by treatment with thrombin, and recover them as single, discrete platelets that aggregate in response to both weak and strong agonists. In the present study we examined the duration of procoagulant activity on the surface of thrombin-degranulated platelets by two methods: a prothrombinase assay, and the binding of 125I-labeled annexin. Control platelets generated 0.9 ± 0.4 U thrombin per 107 platelets in 15 min. Suspensions of thrombin-degranulated platelets formed 5.4 ± 0.1 U thrombin per 107 platelets in this time. Binding of 125I-annexin V was also greater with thrombin-treated platelets than with control platelets (controls: 1.7 ±0.1 ng annexin/107 platelets; thrombin-degranulated platelets: 6.8 ± 0.2 ng annexin/107 platelets). With thrombin-degranulated platelets, increased procoagulant activity and annexin binding persisted for at least 4 h after degranulation and resuspension, indicating that the catalytic activity for the prothrombinase complex is not reversed during this time. These platelets maintained their ability to aggregate for 4 h, even in response to the weak agonist, ADP. Thus, platelets that have taken part in thrombus formation and returned to the circulation may contribute to the promotion of further thrombotic events because of the persistence of procoagulant activity on their surface.

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The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

10.1055/s-0038-1665801 ◽

1979 ◽

Author(s):

H. P. Muller ◽

N. H. van Tilburg ◽

R. M. Bertina ◽

J. J. Veltkamp

Keyword(s):

Molecular Weight ◽

High Salt ◽

Low Molecular Weight ◽

Gel Chromatography ◽

Specific Antibodies ◽

Specific Effects ◽

Normal Plasma ◽

Coagulant Activity ◽

Sterical Hindrance ◽

Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

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Implantation and pregnancy outcome of rats fed with low and high salt diet

Endocrine Abstracts ◽

10.1530/endoabs.38.p361 ◽

2015 ◽

Author(s):

Iranloye Bolanle ◽

Oludare Gabriel

Keyword(s):

Pregnancy Outcome ◽

High Salt ◽

High Salt Diet ◽

Salt Diet

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Enhanced catalytic activity of low-Pt content nanocatalysts supported on hollow carbon spheres for the ORR in alkaline media

MRS Advances ◽

10.1557/adv.2020.370 ◽

2020 ◽

Vol 5 (57-58) ◽

pp. 2961-2972

Author(s):

P.C. Meléndez-González ◽

E. Garza-Duran ◽

J.C. Martínez-Loyola ◽

P. Quintana-Owen ◽

I.L. Alonso-Lemus ◽

...

Keyword(s):

Catalytic Activity ◽

Anion Exchange ◽

Average Particle Size ◽

Synthesis Method ◽

Alkaline Media ◽

High Catalytic Activity ◽

Average Particle ◽

Carbon Spheres ◽

Hollow Carbon ◽

Hollow Carbon Spheres

In this work, low-Pt content nanocatalysts (≈ 5 wt. %) supported on Hollow Carbon Spheres (HCS) were synthesized by two routes: i) colloidal conventional polyol, and ii) surfactant-free Bromide Anion Exchange (BAE). The nanocatalysts were labelled as Pt/HCS-P and Pt/HCS-B for polyol and BAE, respectively. The physicochemical characterization of the nanocatalysts showed that by following both methods, a good control of chemical composition was achieved, obtaining in addition well dispersed nanoparticles of less than 3 nm TEM average particle size (d) on the HCS. Pt/HCS-B contained more Pt0 species than Pt/HCS-P, an effect of the synthesis method. In addition, the structure of the HCS remains more ordered after BAE synthesis, compared to polyol. Regarding the catalytic activity for the Oxygen Reduction Reaction (ORR) in 0.5 M KOH, Pt/HCS-P and Pt/HCS-B showed a similar performance in terms of current density (j) at 0.9 V vs. RHE than the benchmark commercial 20 wt. % Pt/C. However, Pt/HCS-P and Pt/HCS-B demonstrated a 6 and 5-fold increase in mass catalytic activity compared to Pt/C, respectively. A positive effect of the high specific surface area of the HCS and its interactions with metal nanoparticles and electrolyte, which promoted the mass transfer, increased the performance of Pt/HCS-P and Pt/HCS-B. The high catalytic activity showed by Pt/HCS-B and Pt/HCS-P for the ORR, even with a low-Pt content, make them promising cathode nanocatalysts for Anion Exchange Membrane Fuel Cells (AEMFC).

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