ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (3) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (1) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

A new isolation and structure for the endotoxin from Microcystis aeruginosa NRC-1

1970 ◽  
Vol 48 (4) ◽  
pp. 508-510 ◽  
Author(s):  
J. Rama Murthy ◽  
J. B. Capindale
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Solvent Extraction ◽  
Microcystis Aeruginosa ◽  
Green Alga ◽  
Complex Structure ◽  
Strain Analysis ◽  
Blue Green Alga ◽  
Algal Strain ◽  
Toxic Material

The endotoxin from the blue–green alga Microcystis aeruginosa NRC-1 has been isolated as its ammonium salt by a new procedure involving solvent extraction and elution from DEAE-Sephadex A-25. The intraperitoneal LD100 of this toxin preparation for mice was 0.1 mg/kg body weight. The product is a white solid which appears to be chromatographically and electrophoretically homogeneous. This toxin produces similar symptoms in mice to those described originally for the toxic material from the same algal strain. Analysis of the toxin hydrolysate indicates a more complex structure since seven more amino acids have been found, including tyrosine, proline, and arginine, in addition to the seven reported before.

The Effect of Dextran of Various Molecular Weight on the Coagulation in Dogs

1961 ◽  
Vol 06 (01) ◽  
pp. 015-024 ◽  
Author(s):  
Sven Erik Bergentz ◽  
Oddvar Eiken ◽  
Inga Marie Nilsson
Keyword(s):  
Molecular Weight ◽  
Body Weight ◽  
High Molecular Weight ◽  
Bleeding Time ◽  
Factor Vii ◽  
Low Molecular Weight ◽  
Factor V ◽  
Coagulation Mechanism ◽  
Coagulation Defects

Summary1. Infusions of low molecular weight dextran (Mw = 42 000) to dogs in doses of 1—1.5 g per kg body weight did not produce any significant changes in the coagulation mechanism.2. Infusions of high molecular weight dextran (Mw = 1 000 000) to dogs in doses of 1—1.5 g per kg body weight produced severe defects in the coagulation mechanism, namely prolongation of bleeding time and coagulation time, thrombocytopenia, pathological prothrombin consumption, decrease of fibrinogen, prothrombin and factor VII, factor V and AHG.3. Heparin treatment of the dogs was found to prevent the decrease of fibrinogen, prothrombin and factor VII, and factor V otherwise occurring after injection of high molecular weight dextran. Thrombocytopenia was not prevented.4. In in vitro experiments an interaction between fibrinogen and dextran of high and low molecular weight was found to take place in systems comprising pure fibrinogen. No such interaction occurred in the presence of plasma.5. It is concluded that the coagulation defects induced by infusions of high molecular weight dextran are due to intravascular coagulation.

Systemic Thrombin Generation and Activity Resistant to Low Molecular Weight Heparin Administered Prior to Streptokinase in Patients with Acute Myocardial Infarction

1997 ◽  
Vol 77 (01) ◽  
pp. 057-061 ◽  
Author(s):  
Dennis W T Nilsen ◽  
Lasse Gøransson ◽  
Alf-Inge Larsen ◽  
Øyvind Hetland ◽  
Peter Kierulf
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Molecular Weight ◽  
Body Weight ◽  
Low Molecular Weight Heparin ◽  
Troponin T ◽  
Bleeding Complications ◽  
Control Group ◽  
Low Molecular Weight ◽  
Creatine Kinase Mb

SummaryOne hundred patients were included in a randomized open trial to assess the systemic factor Xa (FXa) and thrombin inhibitory effect as well as the safety profile of low molecular weight heparin (LMWH) given subcutaneously in conjunction with streptokinase (SK) in patients with acute myocardial infarction (MI). The treatment was initiated prior to SK, followed by repeated injections every 12 h for 7 days, using a dose of 150 anti-Xa units per kg body weight. The control group received unfractionated heparin (UFH) 12,500 IU subcutaneously every 12 h for 7 days, initiated 4 h after start of SK infusion. All patients received acetylsalicylic acid (ASA) initiated prior to SK.Serial blood samples were collected prior to and during the first 24 h after initiation of SK infusion for determination of prothrombin fragment 1+2 (Fl+2), thrombin-antithrombin III (TAT) complexes, fibrinopeptide A (FPA) and cardiac enzymes. Bleeding complications and adverse events were carefully accounted for.Infarct characteristics, as judged by creatine kinase MB isoenzyme (CK-MB) and cardiac troponin T (cTnT), were similar in both groups of patients.A comparable transient increase in Fl+2, TAT and FPA was noted irrespective of heparin regimen. Increased anti-Xa activity in patients given LMWH prior to thrombolytic treatment had no impact on indices of systemic thrombin activation.The incidence of major bleedings was significantly higher in patients receiving LMWH as compared to patients receiving UFH. However, the occurrence of bleedings was modified after reduction of the initial LMWH dose to 100 anti-Xa units per kg body weight.In conclusion, systemic FXa- and thrombin activity following SK-infusion in patients with acute MI was uninfluenced by conjunctive LMWH treatment.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

scholarly journals Adiponectin: Structure, Physiological Functions, Role in Diseases, and Effects of Nutrition

Nutrients ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 1180
Author(s):  
Kayvan Khoramipour ◽  
Karim Chamari ◽  
Amirhosein Ahmadi Hekmatikar ◽  
Amirhosein Ziyaiyan ◽  
Shima Taherkhani ◽  
...  
Keyword(s):  
Cardiovascular Disease ◽  
Amino Acids ◽  
Molecular Weight ◽  
Energy Regulation ◽  
Treatment Interventions ◽  
Adipose Tissues ◽  
Physiological Functions ◽  
Cellular Events ◽  
Healthy Nutrition

Adiponectin (a protein consisting of 244 amino acids and characterized by a molecular weight of 28 kDa) is a cytokine that is secreted from adipose tissues (adipokine). Available evidence suggests that adiponectin is involved in a variety of physiological functions, molecular and cellular events, including lipid metabolism, energy regulation, immune response and inflammation, and insulin sensitivity. It has a protective effect on neurons and neural stem cells. Adiponectin levels have been reported to be negatively correlated with cancer, cardiovascular disease, and diabetes, and shown to be affected (i.e., significantly increased) by proper healthy nutrition. The present review comprehensively overviews the role of adiponectin in a range of diseases, showing that it can be used as a biomarker for diagnosing these disorders as well as a target for monitoring the effectiveness of preventive and treatment interventions.

ISOLATION OF RAT HEPARIN

1959 ◽  
Vol 37 (1) ◽  
pp. 1183-1186
Author(s):  
L. B. Jaques
Keyword(s):  
Body Weight ◽  
Sodium Salt ◽  
Anticoagulant Activity ◽  
Barium Salt ◽  
Wistar Strain

Heparin was isolated from the whole carcass and skin of rats of the Wistar strain and crystallized as the barium salt. The sodium salt derived from this had a specific anticoagulant activity (Howell assay) of 47.5 International Units/mg and specific metachromatic activity of 101.5 International Units/mg. Yield of heparin was 0.55 mg/100 g body weight.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

Sign in / Sign up

Export Citation Format

Share Document