Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.

BIOTECHNOLOGICAL FEATURES OF PRODUCTION AND QUALITY ASSESSMENT OF LACTOSE-FREE YOGHURT

2021 ◽  
Vol 12 (4) ◽  
Author(s):  
V. Z. Trokhymenko ◽  
M. I. Didukh ◽  
T. I. Kovalchuk ◽  
V. M. Bidenko ◽  
V. V. Zakharin
Keyword(s):  
Physicochemical Properties ◽  
Dairy Products ◽  
Titratable Acidity ◽  
Caloric Content ◽  
Gas Formation ◽  
Sour Milk ◽  
Milk Sugar ◽  
Physico Chemical ◽  
Comparative Aspect ◽  
Chemical Studies

Lactose-free dairy products play a significant role in the diet of people with lactose intolerance, as they are a source of prombiotics and highly nutrients that are readily available, are in balanced proportions and do not contain milk sugar (lactose). In the manufacture of lactose-free dairy products in the technological scheme provides for the extraction of milk sugar (lactose), which can lead to deterioration of their sensory and physicochemical properties. The aim of this work was to study the comparative aspect of biotechnological features of yogurts made by traditional and lactose-free technologies and to evaluate their organoleptic and physicochemical properties. The object of the study were organic drinking yogurt with "blueberry" filler (with probiotic) 2.5 % and lactose-free organic yogurt (with probiotic) 2.5 %. According to the results of research, organic drinking yogurt with "blueberry" filler (with probiotic) 2.5 % in taste was sour milk, without foreign tastes and odors moderately sweet, with a pronounced taste of "blueberry" filler, consistency - homogeneous, tender, dense, without gas formation, with particles of fresh blueberries, which are distributed throughout the mass of yogurt, color - with a shade that is characteristic of blueberries. Organic lactose-free yogurt (with probiotic) 2.5 % had a sour taste, sour milk, without foreign tastes and odors, color - white. According to the results of physico-chemical studies of experimental samples of organic drinking yogurt with "blueberry" filler and lactose-free organic yogurt, the titratable acidity was 80 and 85 oT, active acidity 4.7 and 4.5, respectively. The mass fraction of carbohydrates in drinking yogurt with "blueberry" filler was 9.8 g / 100 g at 4.4 g / 100 g in lactose-free yogurt, including sugar 5.8 and 0 g / 100 g, respectively. Energy value and caloric content was higher in the sample of yogurt with "blueberry" filling. The conditional viscosity of the test samples was 1 min 30 sec. and 59 sec. in accordance. The degree of syneresis in the experimental samples of organic drinking yogurt with the filler "blueberry" and lactose-free organic yogurt was 55 and 45 % moisture content - 44.07 and 39.49 %, respectively.

scholarly journals Physico-Chemical Properties of Deep-Lying Oils

2021 ◽  
Vol 134 (3) ◽  
pp. 11-17
Author(s):  
I. G. Yashchenko ◽  
◽  
Y. M. Polishchuk ◽  
Keyword(s):  
Spatial Distribution ◽  
Physicochemical Properties ◽  
Chemical Properties ◽  
Oil Production ◽  
Urgent Problem ◽  
Physico Chemical ◽  
The World ◽  
Oil Gas

The article is devoted to the urgent problem of studying the features of the properties of poorly studied oils at great depths (more than 4,500 m), the need for development of which is caused by the continuing decline in oil production in traditional oil producing provinces. The analysis of the spatial distribution of reserves across the continents and countries of deep-seated oils and changes in their physico-chemical properties and the occurrence conditions, which made it possible to identify their main features. The studies used information on 21067 oil samples from 167 oil-bearing basins of the world, obtained from the database on the physicochemical properties of oils. The features of the physicochemical properties of deep-seated oils have been established, which are manifested in a decrease in the density and viscosity of oils, in a decrease in the content of sulfur and asphalt-resinous substances, and in an increase in the content of light fractions and oil gas in comparison with oils of small and medium depths.

scholarly journals ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE

1962 ◽  
Vol 115 (3) ◽  
pp. 623-639 ◽  
Author(s):  
J. L. Fahey ◽  
Brigitte A. Askonas
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Gamma Globulin ◽  
Immunological Methods ◽  
Antigenic Determinants ◽  
Antibody Activity ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Γ Globulins ◽  
Starch Gel

Gamma globulin and antibody obtained from inbred C3H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S20,w = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal γ-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original γ-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact γ-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal γ-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The γ-myeloma protein (5563) formed in a C3H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal γ-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal γ-globulin fragments. Although the γ-myeloma protein shares antigenic determinants with normal γ-globulins it lacks some of the antigenic groupings present in the γ-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal γ-globulin. In addition, both S and F fragments of normal γ-globulin possess antigenic groupings not present in fragments of the γ-myeloma protein, accounting for the antigenic deficiency observed on comparison of the γ-myeloma protein with normal γ-globulins.

PHYSICO-CHEMICAL AND GEOCHEMICAL PROPERTIES OF SOILS UNDER SAWAH SYSTEM OF INLAND VALLEYS IN NIGERIA

2019 ◽  
Vol 18 (1) ◽  
pp. 69-86
Author(s):  
C. I. ALARIMA ◽  
M. A. BUSARI ◽  
J. M. AWOTUNDE ◽  
O. O. OLANIYI ◽  
T. MASUNAGA ◽  
...  
Keyword(s):  
Sandy Loam ◽  
Agricultural Practices ◽  
Total Carbon ◽  
Rapid Loss ◽  
Mobile Species ◽  
Geochemical Properties ◽  
Physico Chemical ◽  
Exchangeable Ca ◽  
Extreme Degree ◽  
Basic Cations

This study investigated the physico-chemical and geochemical properties of soils under sawah in Nigeria. It was found that soils under sawah were majorly sandy loam to sandy clay loam having acidic reactions, low exchangeable Ca, Mg, K and Na. These soils were deficient in available P, SiO2, S, Total Nitrogen and Total Carbon while SiO2, Al2O3 and Fe2O3 dominated total elemental composition, accounting for a cumulative average of 96.16%. Except total elemental TiO2 and K2O which showed average values >1%, MnO, MgO, CaO, Na2O and P2O5 showed average values <1%. Soils under sawah exhibited intermediated to extreme weathering degree with majority of the soil sampled falling into the category of extreme weathering. With extreme degree of weathering, rapid loss of mobile species such as basic cations from soil is imminent which may account for the results observed in this study. Thus, combination of conservative agricultural practices is recommended.    

scholarly journals Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

RSC Advances ◽  
2019 ◽  
Vol 9 (34) ◽  
pp. 19828-19836 ◽  
Author(s):  
Li Yuan ◽  
Jiamei Yu ◽  
Jianlou Mu ◽  
Tong Shi ◽  
Quancai Sun ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Silver Carp ◽  
Chemical Properties ◽  
Konjac Glucomannan ◽  
Hypophthalmichthys Molitrix ◽  
Physico Chemical

This work studied the effects of KGM with different degrees of deacetylation (DDs) on the physicochemical properties of silver carp (Hypophthalmichthys molitrix) surimi gels.

Immunological Cross Reaction Between Chains of Human Fibrinogen

1975 ◽  
Author(s):  
B. Oårdlund
Keyword(s):  
Electrophoretic Mobility ◽  
Thick Layer ◽  
Strong Reaction ◽  
Human Fibrinogen ◽  
Crossed Immunoelectrophoresis ◽  
Antigenic Sites ◽  
Barbital Buffer ◽  
Β Chain ◽  
Immunological Cross Reaction ◽  
Chain Variant

Employing the crossed immunoelectrophoresis technique (CIE) the antigenic composition of fibrinogen chains and heterogeneity in their electrophoretic mobility was investigated.Highly purified chains of fibrinogen were prepared by chromatography on CM-cellulose (1). Antisera against chains were prepared by immunizing rabbits with Aα, Bβ and γ chains respectively. The CIE was performed on 10 × 10 glass plates with an 1 mm thick layer of 1% agarose in 0.04 M barbital buffer pH 8.6. The electrophoresis was run for 1 h with 12 V/cm. Four fifth of the gel was cut off and replaced with the same agarose solution containing antibodies. The second dimension electrophoresis was run for about 20 h with 2 V/cm.Using anti Bβ chain serum a partial immunological identity was revealed between the Bβ chain and the γ chain. The Bβ chain has except for the antigenic sites in common with the γ chain additional sites that are unique for the B β chain. The results were confirmed with the anti γ chain serum which gave a strong reaction with both the γ chain and the B β chain preparations. The Aα chain did not react with γ antiserum, nor did the γ chain react with anti Aα chain serum. The immunological relation between the Aα chain and the B β chain is under investigation.These experiments also concluded that the γ chain preparation is contaminated with a B β chain variant that has an electrophoretic mobility similar to that of the γ chain. Also the Bβ chain seemed to be impure due to contamination by an Aα chain derivative with higher electrophoretic mobility.(1) Murano, G., Wiman, B., Blomböck, B. and Blomböck, M. : Preparation and isolation of the S-carboxymethyl derivative chains of human fibrinogen. F.E.B.S. Letters: 14, 37, 1971.

scholarly journals Preformulation Studies of Pralidoxime Chloride for Formulation Development of Microspheres

2019 ◽  
Vol 9 (4-s) ◽  
pp. 338-342
Author(s):  
Shyam Bihari Sharma ◽  
Suman Jain ◽  
K. Ganesan
Keyword(s):  
Melting Point ◽  
Physicochemical Properties ◽  
Dosage Form ◽  
Chemical Parameter ◽  
New Drug ◽  
Physico Chemical ◽  
Pralidoxime Chloride ◽  
Preformulation Studies ◽  
Preformulation Study ◽  
Excipient Compatibility

Microspheres are one of the novel drug delivery system which possess several applications and are made up of assorted polymers. Microspheres can be defined as solid, approximately spherical particles ranging in size from 1 to 1000 μm range in diameter having a core of drug and entirely outer layers of polymers as coating material. They are made up of polymeric, waxy or other protective materials i.e. biodegradable synthetic polymer and modified natural products such as starches, gums, proteins, fats and waxes. Preformulation is a group of studies that focus on the physicochemical properties of a new drug candidate that could affect the drug performance and the development of a dosage form. This couldprovide important information for formulation design or support the need for molecular modification. Every drug has intrinsic chemical and physical properties which has been consider before development of pharmaceutical formulation. This property provides the framework for drugs combination with pharmaceutical ingredients in the fabrication of dosage form. Objective of preformulation study is to develop the elegant, stable, effective and safe dosage form by establishing kinetic rate profile, compatibility with the other ingredients and establish Physico-chemical parameter of new drug substances. The purpose of the present study was to systematically investigate some of the important physicochemical properties of pralidoxime chloride for preparation of microspheres. The physicochemical properties such as solubility, pKa, dissolution, melting point, assay development, excipient compatibility etc. of pralidoxime chloride was carried out. Before selection of excipients, the Preformulation study of drug pralidoxime is completed for successful formulation of microspheres. The result of Preformulation studies shows good flow properties, excipient compatibility, solubility efficiency and melting point. From this study we concluded that pralidoximewith HPMC and EC can be used to formulate pralidoxime microspheres for modified release. Keywords: Microspheres, Preformulation, Pralidoxime chloride, Physico-chemical parameter.

Modeling Physico-chemical Properties of Quinolone Derivatives Using GA-MLR as a Computational Study

2019 ◽  
Vol 15 ◽  
Author(s):  
Meysam Shirmohammadi ◽  
Esmat Mohammadinasab ◽  
Zakiyeh Bayat
Keyword(s):  
Refractive Index ◽  
Physicochemical Properties ◽  
Energy Gap ◽  
Computational Study ◽  
Chemical Properties ◽  
Theoretical Models ◽  
Lumo Energy ◽  
Physico Chemical ◽  
Leave One Out ◽  
Homo Lumo

: In the present study the applicability of various molecular descriptors was tested for the QSPR study on 40 quinolones derivatives. The relationship between some of the molecular indices with physicochemical properties such as refractive index (n), polarizability (α) and HOMO-LUMO energy gap (ΔEH-L) was represented. At first, the chemical structure of quinolones derivatives was optimized by Gaussian 98 program and ab initio method at the #HF/6-31++G**level, and then the physicochemical properties such as refractive index, polarizability and HOMO-LUMO energy gap were calculated. Genetic algorithm using multiple linear regression (GA-MLR) with backward method by SPSS software was used for obtaining properties. The analytical powers of the established theoretical models were discussed using leave-one-out (LOO) cross-validation technique. A multi-parametric equation containing maximum three descriptors with suitable statistical qualities was obtained for predicting the studied properties.

Ontogenetic Variation in the Multiple Hemoglobins of Arctic Charr, Salvelinus alpinus

1989 ◽  
Vol 46 (5) ◽  
pp. 804-809 ◽  
Author(s):  
M. A. Giles ◽  
D. M. Rystephanuk
Keyword(s):  
Life Cycle ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Salvelinus Alpinus ◽  
Arctic Charr ◽  
Ontogenetic Variation ◽  
Starch Gel Electrophoresis ◽  
Free Swimming ◽  
Total Hemoglobin ◽  
Starch Gel

Changes during development in the multiple hemoglobins of hatchery-reared Arctic charr, Salvelinus alpinus, that originated from an anadromous stock from Nauyuk Lake, Northwest Territories were examined by starch gel electrophoresis. A total of 10 anodic and 7 cathodic hemoglobins were expressed during the life cycle of the charr. Embryos and newly-hatched alevins exhibited 10 anodic and 3 cathodic components. Of these embryonic hemoglobins, 5 anodic components and possibly 1 cathodic component with similar electrophoretic mobility were observed in older fish. In free-swimming fry 3–4 new cathodic components were expressed. Two phenotypes (designated as 3-C or 5-C) were identified in postembryonic charr, distinguished by the presence of either 3 or 5 cathodic hemoglobins, respectively. In both phenotypes the proportion of cathodic hemoglobins increased progressively with age to a maximum of 22 and 18% of total hemoglobin in the 3-C and 5-C phenotypes, respectively.

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