A COMPARATIVE STUDY OF THE PROTEINS IN NORMAL MECONIUM AND IN MECONIUM FROM MECONIUM ILEUS PATIENTS

1965 ◽  
Vol 43 (3) ◽  
pp. 381-397 ◽  
Author(s):  
Harry Schachter ◽  
Gordon H. Dixon
Keyword(s):  
Proteolytic Enzymes ◽  
Electrophoretic Pattern ◽  
Dry Weight ◽  
Bound State ◽  
Meconium Ileus ◽  
Starch Gel Electrophoresis ◽  
Direct Role ◽  
Low Viscosity ◽  
Phenol Extraction ◽  
Protein Components

Starch gel electrophoresis and immunoelectrophoresis have been used to confirm previous reports that the highly viscous meconium obtained from patients with meconium ileus is rich in albumin and also contains alpha-, beta-, and gamma-globulins. Normal meconium contains only small amounts of these proteins. It is shown that normal meconium contains a TCA-soluble mucoprotein that is resistant to digestion by the combined action of the proteolytic enzymes trypsin and chymotrypsin. Meconium ileus meconium contains this mucoprotein component in a bound state; it can be released by proteolytic digestion with trypsin and chymotrypsin, or by phenol. Enzymic digestion of meconium ileus meconium destroys all the protein components of abnormal meconium except the resistant mucoprotein, thereby converting the electrophoretic pattern of meconium ileus meconium into a normal pattern. It is suggested that meconium ileus meconium is identical with the contents of the upper small bowel of any normal fetus and that meconium ileus can result when the mechanism of intestinal proteolysis is defective. In an attempt to determine whether meconium ileus meconium contains an abnormal mucoprotein that may be responsible for the viscosity of this material, phenol extraction was used to prepare the mucoprotein from both normal meconium and meconium ileus meconium. About 25% of the dry weight of normal meconium consists of this mucoprotein but the yield of mucoprotein from abnormal meconium is only 2–6% of the dry weight. The relatively low viscosity of mucoprotein from meconium ileus meconium and its presence in only small amounts in the abnormal meconium indicate that it does not play a direct role in the etiology of meconium ileus. The chemical composition of this mucoprotein shows it to be a sialomuco-polysaccharide. Although there are consistent differences between preparations from normal and abnormal meconium, these differences are attributed to partial proteolysis of mucoprotein in the normal digestive tract and are probably not related to cystic fibrosis.

FURTHER STUDIES OF CHANGES IN PLASMA PROTEINS IN AVIAN ERYTHROBLASTOSIS: II. INVOLVEMENT OF α-LIPOPROTEIN

1965 ◽  
Vol 43 (10) ◽  
pp. 1667-1675 ◽  
Author(s):  
Mohendra Merriman ◽  
C. le Q. Darcel
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Electrophoretic Pattern ◽  
Starch Gel Electrophoresis ◽  
Normal Plasma ◽  
Starch Gel ◽  
Protein Components

Earlier studies with paper and starch gel electrophoresis of plasma from birds with erythroblastosis indicated an alteration in the mobility of one of its protein components. This protein has now been shown to be α-lipoprotein. Efforts have been made to simulate leukemic changes experimentally in normal plasma. Of all the treatments and materials tried, only incubation with turpentine and pinene compounds produced alterations in the electrophoretic pattern closely resembling those in leukemia.

scholarly journals Starch-Gel Electrophoresis of Wheat Flour Proteins

1963 ◽  
Vol 16 (2) ◽  
pp. 342 ◽  
Author(s):  
Janet SD Graham
Keyword(s):  
Acetic Acid ◽  
Wheat Flour ◽  
Gel Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Similar Protein ◽  
Starch Gel ◽  
Protein Components ◽  
Electrophoresis Of Proteins

An improved apparatus and procedures for starch-gel electrophoresis of proteins of wheat flour are described; highly reproducible separation of the protein components was achieved. By starch-gel electrophoresis it was shown that similar protein components occur in the extracts of wheat flour obtained with a variety of solvents; however, there were marked differences in the proportions of these components in various extracts. Several protein components were present in the fJ'actions separated by ion-exchange chromatography of' the proteins soluble in Bodium pyrophosphate and of those soluble in acetic acid; some fractions containeda number of similar protein components.

Growth and proteinase production inPseudomonasspp. cultivated under various conditions of temperature and nutrition

1968 ◽  
Vol 35 (3) ◽  
pp. 385-393 ◽  
Author(s):  
H. S. Juffs ◽  
A. C. Hayward ◽  
H. W. Doelle
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Organic Nitrogen ◽  
Proteolytic Enzymes ◽  
Dry Weight ◽  
Growth Cycle ◽  
Logarithmic Phase ◽  
Proteinase Production

SummaryA study was made of the formation of the extracellular proteolytic enzymes during the growth cycle of several species ofPseudomonascultivated under different conditions of temperature and nutrition. Proteolytic activity was not proportional to growth. Expressed per unit of cell dry weight, the proteolytic activity showed a peak in the early logarithmic phase which was greater in cultures grown at 3 than at 28°C. Proteolytic enzyme was not formed in the absence of organic nitrogen. Of 16 organisms studied,Pseudomonas aeruginosaATCC 10145 was the most prolific producer of proteolytic enzyme.

Electrophoretic Analysis of Polypeptides of Plasma Membranes from Bovine Pituitary Gland

1974 ◽  
Vol 52 (7) ◽  
pp. 620-630
Author(s):  
André Lemay ◽  
Fernand Labrie
Keyword(s):  
Plasma Membranes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Broad Band ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Apparent Molecular Weight ◽  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Protein Components ◽  
Membrane Components

Purified plasma membranes from bovine hypophyseal tissue have been fractionated by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis under various conditions of pH and acrylamide concentrations. The best separation of protein components is achieved at a concentration of 7.5% acrylamide and at pH 7.1. Under these conditions, the electrophoretic pattern consistently shows 36 protein bands ranging in molecular weights from 250 000 to 15 000. Only one broad band, having an apparent molecular weight of 150 000, stains for glycoproteins by the period acid – Schiff technique. After electrophoresis on a two-dimensional polyacrylamide gel system using disc gels containing urea and Triton X-100 in the first dimension and SDS in the second dimension, approximately 45 different protein components can be identified. Less than 12% of the membrane proteins are solubilized by washing the membranes with 1 M KCl or NH4Cl. Denaturating agents like urea and lithium 3,4-diiodosalycilate solubilize 55–60% of membrane components. Adenohypophyseal plasma membranes show an eleetrophoretic pattern completely different from that obtained with membranes isolated from the intermediate or posterior pituitary lobes.

scholarly journals Electron Tomography Reveals Posttranscriptional Binding of Pre-Mrnps to Specific Fibers in the Nucleoplasm

2000 ◽  
Vol 148 (2) ◽  
pp. 271-282 ◽  
Author(s):  
Francesc Miralles ◽  
Lars-Göran Öfverstedt ◽  
Nafiseh Sabri ◽  
Youssef Aissouni ◽  
Ulf Hellman ◽  
...  
Keyword(s):  
Electron Tomography ◽  
Protein Composition ◽  
Bound State ◽  
Specific Protein ◽  
Nuclear Pore ◽  
Splicing Factors ◽  
Free Diffusion ◽  
Hnrnp Proteins ◽  
Protein Components ◽  
In Transit

Using electron tomography, we have analyzed whether the Balbiani ring (BR) pre-mRNP particles in transit from the gene to the nuclear pore complex (NPC) are bound to any structure that could impair free diffusion through the nucleoplasm. We show that one-third of the BR particles are in contact with thin connecting fibers (CFs), which in some cases merge into large fibrogranular clusters. The CFs have a specific protein composition different from that of BR particles, as shown by immuno-EM. Moreover, we have identified hrp65 as one of the protein components of the CFs. The sequencing of hrp65 cDNA reveals similarities with hnRNP proteins and splicing factors. However, hrp65 is likely to have a different function because it does not bind to nascent pre-mRNA and is not part of the pre-mRNP itself. Taken together, our observations indicate that pre-mRNPs are not always freely diffusible in the nucleoplasm but interact with fibers of specific structure and composition, which implies that some of the posttranscriptional events that the pre-mRNPs undergo before reaching the NPC occur in a bound state.

scholarly journals COLLAGEN EXTRACTION FROM YELLOWFIN TUNA (Thunnus albacares) SKIN AND ITS ANTIOXIDANT ACTIVITY

2019 ◽  
Vol 81 (2) ◽  
Author(s):  
Mala Nurilmala ◽  
Shita Fauzi ◽  
Dian Mayasari ◽  
Irmanida Batubara
Keyword(s):  
Antioxidant Activity ◽  
Acetic Acid ◽  
Sodium Hydroxide ◽  
Type I Collagen ◽  
Electrophoretic Pattern ◽  
Dry Weight ◽  
Butyl Alcohol ◽  
Type I ◽  
Acid Soluble Collagen ◽  
Skin Collagen

Tuna skin, a byproduct of the fish processing industry, is used as an alternative collagen source to replace bovine and porcine products. This study aimed to extract collagen from tuna skin with acetic acid, and investigated the antioxidant activity. Collagen extraction was carried out through a pretreatment process, defatted with butyl alcohol, and soaking in acetic acid to extract the Acid Soluble Collagen (ASC). The effect of concentration of sodium hydroxide and soaking time on the non-collagenous protein removed were measured, and evaluated. The yield and antioxidant activity of each sample were evaluated and the best result was determined by ANOVA. The highest yield of collagen was 3.18% based on dry weight reached at the treatment with sodium hydroxide 0.2 M and acetic acid 1 M. The different treatments did not result in any significant differences in the spectrum of amide A, B, I, II and III which are the characteristics spectra of collagen. Based on the electrophoretic pattern, tuna skin collagen has two  chains (1 and 2), and one β chain. Therefore, it is classified as type I collagen. The main amino acids were glycine and proline. In addition, the strongest antioxidant activity was found in the sample treated with sodium hydroxide 0.05 M and acetic acid 1 M treatment with IC50 value of 0.45 mg/mL. This study is the first to report on antioxidant activity from fish collagen (not hydrolysate or peptide products).

Quantitative Bausteinanalyse der Stützmembran in der Zellwand von Escherichia coli B

1962 ◽  
Vol 17 (3) ◽  
pp. 190-196 ◽  
Author(s):  
H. H. Martin ◽  
H. Frank
Keyword(s):  
Cell Wall ◽  
Proteolytic Enzymes ◽  
Diaminopimelic Acid ◽  
Chemical Compositions ◽  
Balance Sheets ◽  
E Coli ◽  
Molar Ratios ◽  
Rigid Layer ◽  
Protein Components ◽  
Escherichia Coli B

The three concentric layers of the cell wall of E. coli B (the outer lipoprotein layer, the intermediate lipopolysaccharide layer and the inner protein- and mucopolymer containing rigid layer) contribute 60%, 12% and 21%, respectively, to the total weight of the cell wall. — Treatment of the rigid layer with proteolytic enzymes removes the bulk of its protein components but leaves it otherwise intact: still rigid and cell-shaped, it is found to contain glucose, lipid and the mucopeptide constituents muramic acid, glucosamine, diaminopimelic acid, glutamic acid and alanine in molar ratios corresponding to the chemical compositions of known enzymatic mucopolymer split-products from E. coli-walls. Quantitative balance sheets of these components are made up and their implications on the structural concept of the rigid layer are discussed.

Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1317-1320 ◽  
Author(s):  
E. kaminski ◽  
W. Bushuk
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Direct Detection ◽  
Proteolytic Enzymes ◽  
Urea Concentration ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Multiple Forms ◽  
Starch Gel ◽  
Sensitive Method

A rapid and sensitive method for the direct detection of multiple forms of proteolytic enzymes by starch gel electrophoresis is described. The location of the enzyme components is identified by the degradation of hemoglobin which is included in the starch gel. This method was used to identify the enzyme components of the 10 commercial proteolytic enzymes bromelain, chymotrypsin, ficin, papain, pepsin, pronase B, protease, proteinase, and two preparations of trypsin. The effects of urea concentration and the ionic strength of aluminium lactate buffer were also examined. The best results were obtained with 3 M urea and with an ionic strength of 0.1 for the lactate buffer. It was observed that the number of enzyme components decreased with increasing concentrations of urea or increasing ionic strength of lactate buffer. The number of enzyme components did not always correspond to the number of protein bands. Self-digestion occurred in some of the protein bands in the starch gel after electrophoretic separation of the proteolytic enzymes.

scholarly journals Physical, Chemical and Rheological Characterization of Tuber and Starch from Ceiba aesculifolia subsp. parvifolia

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2097
Author(s):  
Lizette Suastegui-Baylón ◽  
Ricardo Salazar ◽  
Yanik I. Maldonado-Astudillo ◽  
Manuel O. Ramírez-Sucre ◽  
Gerónimo Arámbula-Villa ◽  
...  
Keyword(s):  
Food Systems ◽  
Antioxidant Properties ◽  
Thermal Characteristics ◽  
High Hardness ◽  
Dry Weight ◽  
Morphological Properties ◽  
Rheological Characterization ◽  
Low Viscosity ◽  
Physical Chemical ◽  
Ceiba Aesculifolia

This work aimed to evaluate the physical, chemical and antioxidant properties of Ceiba aesculifolia subsp. parvifolia (CAP) tuber and determinate rheological, thermal, physicochemical and morphological properties of the starch extracted. The CAP tuber weight was 3.66 kg; the edible yield was 82.20%. The tuber presented a high hardness value (249 N). The content of carbohydrates (68.27%), crude fiber (15.61%) and ash (9.27%) from the isolated starch, reported in dry weight, were high. Phenolic compounds and flavonoid content of CAP tuber peel were almost 3-fold higher concerning the pulp. CAP tuber starch exhibited a pseudoplastic behavior and low viscosity at concentrations of 5–15%. Purity percentage and color parameters describe the isolated starch as high purity. Thermal characteristics indicated a higher degree of intermolecular association within the granule. Pasting properties describes starch with greater resistance to heat and shear. CAP tuber starch has X-ray diffraction patterns type A. The starch granules were observed as oval and diameters ranging from 5 to 30 µm. CAP tuber could be a good source of fiber and minerals, while its peel could be used for extracting bioactive compounds. Additionally, the starch separated from this tuber could be employed as a thickening agent in food systems requiring a low viscosity and subjected to high temperatures.

scholarly journals Inheritable Differences in the Electrophoretic Pattern of Hemoglobin Revealed in a Local Random-Bred Colony of Albino Rats

Blood ◽  
1970 ◽  
Vol 35 (4) ◽  
pp. 447-450 ◽  
Author(s):  
JOVO V. MARTINOVIC ◽  
DOBRIVOJE V. MARINKOVIC ◽  
DUSAN T. KANAZIR ◽  
PETER N. MARTINOVITCH
Keyword(s):  
Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Albino Rats ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Parental Type ◽  
Starch Gel ◽  
F2 Generation

Abstract In a local colony of random-bred Albino rats, three different patterns of hemoglobin, arbitrarily denoted as patterns I, II and III, were detected by means of starch-gel electrophoresis in a discontinuous buffer system. Mating experiments showed that rats bearing pattern I and pattern III hemoglobin bred true. Crosses of pattern I with pattern III animals yielded only pattern II animals, and when the latter were mated inter se, the resultant F2 generation showed approximately a ratio of 1:2:1 for patterns I, II and III, respectively. When F1 animals from pattern I with pattern III crosses were mated back to animals of either parental type, the resultant ratio was found to be one pattern II: one pattern I or pattern III.

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