HEMAGGLUTININS FROM OYSTER HEMOLYMPH

1967 ◽  
Vol 45 (6) ◽  
pp. 1225-1234 ◽  
Author(s):  
M. F. Li ◽  
Carol Flemming
Keyword(s):  
Gel Filtration ◽  
Water Soluble ◽  
Protein Fractions ◽  
Agar Gel ◽  
Human Red Blood Cells ◽  
Optimum Ph ◽  
Wide Ph Range ◽  
Main Protein ◽  
Ph Range ◽  
Gel Diffusion

Oyster hemolymph hemagglutinin agglutinated fish, rabbit, and human, red blood cells, was active over a wide pH range (optimum pH 7.5), and was heat-labile. Dialysis caused a greater reduction in the activity in the aged hemolymph than it did in the fresh hemolymph. Ultracentrifugation removed 90% of the protein; the remaining 11% retained all the activity. Gel filtration revealed two distinct hemagglutinins associated with two main protein peaks. Fractionation according to solubility gave seven different protein fractions, but only the salt-soluble and a very minor water-soluble Fraction possessed hemagglutinating activity. Agar-gel diffusion tests on the protein fractions showed a complexity of patterns which was partially resolved by immunoelectrophoretic techniques.

scholarly journals Functional properties of sesame (Sesamum indicum Linn) seed protein fractions

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Atinuke O. Idowu ◽  
Adeola M. Alashi ◽  
Ifeanyi D. Nwachukwu ◽  
Tayo N. Fagbemi ◽  
Rotimi E. Aluko
Keyword(s):  
Functional Properties ◽  
Seed Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sesame Seed ◽  
Water Soluble ◽  
Protein Fractions ◽  
Wide Ph Range ◽  
Food Applications ◽  
Ph Range

Abstract This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications. Sesame seed protein fractions were prepared according to their solubility: water-soluble (albumin), salt-soluble (globulin), alkaline-soluble (glutelin) and ethanol-soluble (prolamin). Globulin was the most abundant fraction, consisting of 91% protein, followed by glutelin, albumin and prolamin in decreasing order. Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed polypeptides of sizes ≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19, 85 and 100 kDa. Prolamin had polypeptide sizes 20, 40 and 100 kDa. The albumin and globulin fractions had higher intrinsic fluorescence intensity (FI) values than the glutelin. Albumin had a higher solubility (ranging from 80 to 100%) over a wide pH range when compared with the other fractions. Water holding capacity (g/g) reduced from 2.76 (glutelin) to 1.35 (prolamin) followed by 0.42 (globulin) and 0.08 (albumin). Oil holding capacity (g/g) reduced from: 4.13 (glutelin) to 2.57 (globulin) and 1.56, 1.50 for albumin and prolamin respectively. Gelling ability was stronger for prolamin and glutelin than albumin and globulin, while higher emulsion (p < 0.05) quality was obtained for prolamin and albumin than for glutelin and globulin. Graphical abstract

scholarly journals Digestive Proteases From Fish Processing Wastes: Their Partial Characterization and Comparison

2020 ◽  
Author(s):  
Ivana Soledad Friedman ◽  
Leonel Agustín Behrens ◽  
Nair A Pereira ◽  
Edgardo Contreras ◽  
Analia Verónica Fernández-Gimenez
Keyword(s):  
Residual Activity ◽  
Fish Processing ◽  
Intestinal Enzymes ◽  
Optimum Ph ◽  
Digestive Proteinases ◽  
Wide Ph Range ◽  
Processing Wastes ◽  
Reducing Costs ◽  
Ph Range ◽  
Percophis Brasiliensis

Abstract Fish processing generates a lot of wastes which are discarded resulting in environmental problems. However, this material represents a significant source of high-value bioproducts with potential biotechnological applications. The objective of this study was to characterize and to compare specific activities of acid and alkaline proteases recovered from the viscera of Merluccius hubbsi (Mh), Percophis brasiliensis (Pb), Urophyis brasiliensis (Ub), and Cynoscion guatucupa (Cg) under different pH and temperature conditions. Stomach proteinases from four species had a higher activity at pH 2, with stability in the range of pH 2-4. Optimum pH from intestinal enzymes of Cg was 11.5, while for the crude extract of Mh, Pb, and Ub catalytic activity was registered over a wide pH range range from 7 to 11.5. Stomach proteinases from four studied species had a higher activity at 30 °C and 50 °C, with stability at 10 °C and 30 °C. Optimum temperature from intestinal enzymes of the four tested species was 50 °C with high stability at 10 °C and 30 °C. Alkaline proteinase from all species and acid proteinases from Cg was inactivated at 70ºC, while stomach enzymes of Mh, Pb, and Ub had a residual activity lower than 5% at 80 °C after 5, 10 y 20 minutes of pre-incubation, respectively. Digestive proteinases recovered in this study could be used as biocatalysts in industrial processes, reducing costs, adding value to the fishery waste, and contributing to the reduction of environmental pollution.

Purification and characteristics of the chloride transport stimulating factor from locust corpora cardiaca: a new peptide

1980 ◽  
Vol 58 (10) ◽  
pp. 1851-1860 ◽  
Author(s):  
J. E. Phillips ◽  
W. Mordue ◽  
J. Meredith ◽  
J. Spring
Keyword(s):  
Chloride Transport ◽  
Short Circuit ◽  
Gel Filtration ◽  
Short Circuit Current ◽  
Water Soluble ◽  
Cellulose Acetate Electrophoresis ◽  
Corpora Cardiaca ◽  
Ph Range ◽  
And Storage ◽  
Layer Chromatography

Corpora cardiaca (CC), cAMP, and hemolymph all increase short-circuit current (Isc) and electropotential difference (PD) across locust rectum by stimulating electrogenic transport of Cl− from the lumen. Using ΔIsc as a bioassay, we have purified the water-soluble stimulant (CTSH) from CC using gel filtration chromatography, DEAE-Sephadex anion exchange, cellulose acetate electrophoresis, and thin-layer chromatography. A single peak of CTSH activity was observed after all these procedures, although small amounts of CTSH activity occasionally remained in the high molecular weight (MW) protein precipitate. CTSH was purified more than 100-fold on Bio-Gel P-30 columns. It has a MW of 8 000 – 12 000, is destroyed by trypsin digestion, and has a net negative charge over the pH range (5–10) at which it is most stable. Various properties (i.e., stability at 20 °C, localization in CC, MW, Rf values) and reciprocal bioassay s indicate that CTSH is different from diuretic, antidiuretic, and adipokinetic hormones from locust CC. No difference in the properties of CTSH from glandular (GL) and storage lobes (SL) of CC were noted, although 80% of activity was in the SL. The concentration of purified CTSH required to cause maximal stimulation of rectal Isc is less than 7 nM.

scholarly journals Synthesis of water-soluble chitosan for biomedical applications

2015 ◽  
Vol 18 (3) ◽  
pp. 170-180
Author(s):  
Anh Thi Tram Tu ◽  
Huy Thuc Ha
Keyword(s):  
Drug Delivery ◽  
Molecular Weight ◽  
Iron Oxide ◽  
Biomedical Applications ◽  
Drug Delivery Systems ◽  
Water Soluble ◽  
Oxide Nanoparticles ◽  
Wide Ph Range ◽  
Ft Ir ◽  
Ph Range

Highly deacetylated chitosan (CS) reacted with anhydride acetic (Ac2O) to produce chitosan with various degree of deacetylation (DDA) depending on the CS/Ac2O ratios. The structure of products was characterized by FT-IR, 1H NMR, 13C NMR, and the molecular weight was identified by GPC. The DDA of products decreases as the CS/Ac2O ratio increases. The products with less than 80 % DDA were soluble in water with a wide pH range. The water-soluble chitosan can be used in many biomedical applications such as manufacturing drug delivery systems or functionalized iron oxide nanoparticles.

scholarly journals Screening and Purification of a Chymotrypsin Inhibitor from Entrolobium Saman Seeds

2010 ◽  
Vol 15 ◽  
pp. 19
Author(s):  
Maher Ali. Maqtari ◽  
A.B. Mohamed. Saad
Keyword(s):  
Molecular Weight ◽  
Enzyme Inhibitor ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Molar Ratio ◽  
Apparent Dissociation Constant ◽  
Chymotrypsin Inhibitor ◽  
Ammonium Sulphate Precipitation ◽  
Wide Ph Range ◽  
Ph Range

A chymotrypsin inhibitor was isolated and purified from the seeds of Enterolobium saman  (Leguminaceae family) by extraction with 100 mM phosphate buffer, heat treatment, ammonium sulphate precipitation, ion-exchange chromatography on DEAEcellulose and filtration through Sephadex G-75. The final preparation appeared to be homogeneous by both chromatographic and electrophoretic analyses. ESCI had a molecular weight of about 17,890 and an isoelectric point of 5.8. ESCI inhibited bovine chymotrypsin at an inhibitor-enzyme molar ratio of 1:2. The inhibition mode of chymotrypsin inhibitor was competitive on bovine chymotrypsin. Investigation has been carried out on the complex formed between chymotrypsin and chymotrypsin inhibitor by physico-chemical methods. An apparent dissociation constant (Ki) of 9.05 X 10-8 M has been calculated for the complex. This enzyme-  inhibitor complex was isolated by gel filtration on Sephadex G-75 and a molecular weight of 43.000 was estimated for the complex. The inhibitor did not have any effect on other proteinases, such as papain, bromelin, elastase, α -amylase, trypsin and pepsin. The chemical modification of lysine residues indicated that –NH2  groups are not essential for the activity of ESCI toward chymotrypsin. The inhibitor was an acidic protein and was stable over a wide pH range of 2-12 and temperature range of 10o C-97o C. 

Hydrothermally treated chitosan spontaneously forms water-soluble spherical particles stable at a wide pH range

2016 ◽  
Vol 65 (15) ◽  
pp. 751-758 ◽  
Author(s):  
Srijita Basumallick ◽  
Maria Gabriela Nogueira Campos ◽  
David Richardson ◽  
Andre Gesquiere ◽  
Swadeshmukul Santra
Keyword(s):  
Water Soluble ◽  
Spherical Particles ◽  
Wide Ph Range ◽  
Ph Range

Receptors for sulfate that function across a wide pH range in mixed aqueous–DMSO media

2019 ◽  
Vol 55 (82) ◽  
pp. 12312-12315 ◽  
Author(s):  
Lei Qin ◽  
James R. Wright ◽  
Jakob D. E. Lane ◽  
Stuart N. Berry ◽  
Robert B. P. Elmes ◽  
...  
Keyword(s):  
Water Soluble ◽  
Aqueous Dmso ◽  
Wide Ph Range ◽  
Ph Range

Water soluble macrocyclic squaramides bind selectively to sulfate in aqueous–DMSO mixtures across a pH range from 3.2–14.

A proteolytic pseudomonad from skin lesions of rainbow trout (Salmo gairdnerii). II. Some properties of the proteinase

1968 ◽  
Vol 14 (8) ◽  
pp. 875-880 ◽  
Author(s):  
M. F. Li ◽  
Carol Jordan
Keyword(s):  
Rainbow Trout ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Skin Lesions ◽  
Complexing Agents ◽  
Bivalent Cations ◽  
Wide Ph Range ◽  
Ph Range ◽  
Trout Muscle ◽  
Cellulose Column

An extracellular proteinase from a pseudomonad pathogenic to rainbow trout was purified 33-fold by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G 75 gel filtration. The purified enzyme was active over a wide pH range, from pH 5.0 to 10.0. Heating at 98 °C for 1 h did not completely inactivate the enzyme. Its observed temperature optimum was 45 °C. Michaelis–Menten constants were found to be 0.625% for casein and 0.263% for rainbow trout muscle albumin. Activation energies calculated for these substrates were 8.1 kcal and 11.4 kcal per mole, respectively. The involvement of bivalent cations and free sulfhydryl groups in the enzymatic activity was demonstrated by the inhibition caused by metal-complexing agents and p-chloromercuribenzoate, respectively.

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