Studies on the reactions of animals to infestation with ticks. IV. The protein components of tick extracts

1959 ◽  
Vol 10 (4) ◽  
pp. 604 ◽  
Author(s):  
RF Riek
Keyword(s):  
Filter Paper ◽  
Protein Composition ◽  
Paper Electrophoresis ◽  
Boophilus Microplus ◽  
Laboratory Animals ◽  
Egg Extract ◽  
Egg Extracts ◽  
Protein Components ◽  
The Individual ◽  
Eggs And Larvae

Filter-paper and starch electrophoresis and gel diffusion have been used to separate and identify the various protein components of tick extracts. Changes in the relative protein composition with increasing age of the eggs and larvae of Boophilus microplus (Canestrini) were revealed on filter paper electrophoresis. Toxicity of laboratory animals was due on most occasions to three fractions, F1, F2, and F6, in the egg extract, but to only one fraction, F2–3, in the larval extract. On a few occasions the a-globulin, F6 (haemixodovin), was non-toxic. The reason for the apparent variation in toxicity of this fraction is not understood. Toxicity decreased with age of both eggs and larvae, 14-day-old larvae being relatively non-toxic. Reactions of identity revealed the presence of similar or closely related components in the egg and larval extracts. Immunization with larval extracts prevented the toxic effects of the egg extracts. The antigen largely responsible for the development of skin hypersensitivity, F1, was also one of the toxic components. It was a y-globulin and had the greatest mobility of the y-globulins under these specified electrophoretic conditions. Skin-sensitizing activity was also shown by fraction F2, and to a lesser degree by F3. This may have been due to incomplete separation of the individual components.

Heat stability of homogenized milk: role of interfacial protein

1994 ◽  
Vol 61 (4) ◽  
pp. 507-516 ◽  
Author(s):  
Catharina H. McCrae ◽  
David Hirst ◽  
Andrew J. R. Law ◽  
D. Donald Muir
Keyword(s):  
Serum Protein ◽  
Protein Interactions ◽  
Protein Composition ◽  
Surface Protein ◽  
Heat Stability ◽  
Protein Protein Interactions ◽  
Ph Profile ◽  
Protein Components ◽  
The Individual

SummaryThe role of interfacial protein in determining the heat stability of recombined milk was investigated by removing serum protein prior to homogenization and reincorporating it after homogenization. In addition, the surface protein composition of recombined fat globules was probed by analyses of protein load and by quantification of the individual surface protein components using FPLC. In the absence of serum protein, substantially more casein was bound to the fat surface during homogenization. Despite this, the detrimental effect of homogenization on heat stability did not occur when serum protein had been removed from the system. Reincorporation of serum protein after homogenization caused the heat coagulation time–pH profile to revert to a form very similar to that observed without removing serum protein from the system. Thus, adsorption of serum protein did not affect heat stability. It is more likely that heat-induced interactions of serum protein with surface-adsorbed casein promoted heat coagulation. Fat surface area rather than casein load affected these interfacial protein-protein interactions during heating.

Studies of Casein. I. Some Observations on the Heterogeneity of Casein Fractions

1959 ◽  
Vol 12 (4) ◽  
pp. 712 ◽  
Author(s):  
HA McKenzie ◽  
RG Wake
Keyword(s):  
Filter Paper ◽  
Paper Electrophoresis ◽  
The Other ◽  
Minor Components ◽  
Casein Micelles ◽  
Protective Colloid ◽  
Alcohol Fraction ◽  
Minor Protein ◽  
Fractionation Method ◽  
Protein Components

The heterogeneity of casein is discussed in the light of methods currently used for the fractionation of casein. In particular, the possible heterogeneity of certain preparations of α-casein is considered. This is important because it has been generally considered that α-casein is the protective colloid which is altered when the enzyme, rennin, acts on casein micelles. Recently, Waugh and von Hippel (1956) have suggested that their new component x-casein, and not α-casein, is the protective colloid. These two viewpoints could be reconciled if α-casein samples previously examined contained x-casein as well. In the present work, a study is made of filter paper electrophoresis, micelle-forming properties, and sedimentation of casein fractions. It is shown that x-casein is concentrated with α-casein in fraction A during the alcohol fractionation method of Hipp et al. (1952). On the other hand fraction B contains α-casein essentially free of x-casein. The a-casein obtained in the urea fractionation method of Hipp et al. also contains x-casein. Thus only alcohol fraction B is a suitable source of pure α-casein. During the paper electrophoretic examination of casein fractions a number of minor protein components are observed. A component moving more slowly than γ-casein is present in acid casein, second-cycle casein-fraction P, and an alcohol fraction. This component was first observed in the latter fraction by Hipp et al. (1952) when preparing γ-casein. Electropherograms of second-cycle casein-fraction S indicate the presence of x-, β-, and γ-casein, and two minor components moving between x- and β The way in which these components arise is briefly discussed.

Studies on the reactions of animals to infestation with ticks. II. Tick toxins

1957 ◽  
Vol 8 (2) ◽  
pp. 215 ◽  
Author(s):  
RF Riek
Keyword(s):  
Clinical Syndrome ◽  
Ixodid Ticks ◽  
Laboratory Animals ◽  
Dose Rates ◽  
Ixodes Holocyclus ◽  
Initial Rise ◽  
Egg Extract ◽  
Egg Extracts ◽  
The One ◽  
Tick Paralysis

Toxin has been shown to be present in the eggs of 17 species of ixodid ticks, and is probably present in the eggs of all species of this family. It was associated with the globulin fraction of the egg extract, and was thermolabile. Similar toxin was also present in the larvae of the only four species of ixodid ticks of which larvae were tested. The toxin was not present in the eggs of the five species of argasid ticks used in this study. Clinical syndrome and the pathological changes in the tissues of laboratory animals following injection of egg extracts were indicative of toxaemia. At a dose rate of 0.3 g/kg body weight, there was a rapid initial rise in rectal temperature, followed by subnormal temperature and death. At lower dose rates, there was loss of hair a t the site of injection, and usually the development of an indurated, sterile ulcer. The toxin appeared to be quite distinct from the one that causes tick paralysis, which, in Australia, results from infestation with Ixodes holocyclus Neumann.

A STUDY OF THE PROTEINS IN THE FOLLICULAR FLUID OF THE COW

1957 ◽  
Vol 15 (3) ◽  
pp. 273-NP ◽  
Author(s):  
R. CARAVAGLIOS ◽  
R. CILOTTI
Keyword(s):  
Blood Serum ◽  
Follicular Fluid ◽  
Protein Composition ◽  
Paper Electrophoresis ◽  
Total Proteins ◽  
Protein Components

SUMMARY The protein composition of the follicular fluid of the cow has been investigated. Paper electrophoresis showed that the protein components were qualitatively similar to those of blood serum, although there were some quantitative differences. Thus albumin levels are greater in follicular fluid than in serum, while α2- and γ2-globulins are lower in the former. β-Lipoproteins are not detectable in the follicular fluid. The ratio between total proteins and some glycoproteins is similar in both fluids. The significance of these results in relation to the origin of the follicular fluid is discussed.

Cholesterol in Serum and Lipoprotein Fractions

1956 ◽  
Vol 2 (3) ◽  
pp. 145-159 ◽  
Author(s):  
Joseph T Anderson ◽  
Ancel Keys
Keyword(s):  
Human Serum ◽  
Total Cholesterol ◽  
Filter Paper ◽  
Room Temperature ◽  
Paper Electrophoresis ◽  
Cholesterol Content ◽  
Intraindividual Variability ◽  
Detailed Data ◽  
The Stability ◽  
Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

scholarly journals The Michigan BioTrust for Health: Using Dried Bloodspots for Research to Benefit the Community While Respecting the Individual

2011 ◽  
Vol 39 (S1) ◽  
pp. 98-101 ◽  
Author(s):  
Denise Chrysler ◽  
Harry McGee ◽  
Janice Bach ◽  
Ed Goldman ◽  
Peter D. Jacobson
Keyword(s):  
Public Health ◽  
Community Health ◽  
Filter Paper ◽  
Health Program ◽  
The State ◽  
Public Health Laboratory ◽  
Public Health Program ◽  
Personal Use ◽  
The Individual ◽  
Blood Spot

The Michigan Department of Community Health (MDCH) stores almost 4 million dried blood spot specimens (DBS) in the Michigan Neonatal Biobank. DBS are collected from newborns under a mandatory public health program to screen for serious conditions. At 24 to 36 hours of age, a few drops of blood are taken from the baby’s heel and placed on a filter paper card. The card is sent to the state public health laboratory for testing. After testing, MDCH retains the spots indefinitely for the personal use of the patient and also, pursuant to a 2000 law, for possible research.

Localization of Protein-bound Radioactive Iodine by Filter Paper Electrophoresis

Science ◽  
1952 ◽  
Vol 115 (2997) ◽  
pp. 626-627 ◽  
Author(s):  
F. Larson ◽  
W. P. Deiss ◽  
E. C. Albright
Keyword(s):  
Filter Paper ◽  
Radioactive Iodine ◽  
Paper Electrophoresis

scholarly journals Simulated Breathing: Application of Molecular Dynamics Simulations to Pulmonary Lung Surfactant

Symmetry ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1259
Author(s):  
Maksymilian Dziura ◽  
Basel Mansour ◽  
Mitchell DiPasquale ◽  
P. Charukeshi Chandrasekera ◽  
James W. Gauld ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Pulmonary Surfactant ◽  
Lung Surfactant ◽  
Protein Composition ◽  
Md Simulations ◽  
Building Blocks ◽  
Future Research ◽  
Total Composition ◽  
Protein Components ◽  
Dynamics Simulations

In this review, we delve into the topic of the pulmonary surfactant (PS) system, which is present in the respiratory system. The total composition of the PS has been presented and explored, from the types of cells involved in its synthesis and secretion, down to the specific building blocks used, such as the various lipid and protein components. The lipid and protein composition varies across species and between individuals, but ultimately produces a PS monolayer with the same role. As such, the composition has been investigated for the ways in which it imposes function and confers peculiar biophysical characteristics to the system as a whole. Moreover, a couple of theories/models that are associated with the functions of PS have been addressed. Finally, molecular dynamic (MD) simulations of pulmonary surfactant have been emphasized to not only showcase various group’s findings, but also to demonstrate the validity and importance that MD simulations can have in future research exploring the PS monolayer system.

Stage-specific patterns of collagen gene expression during development of Caenorhabditis elegans

1985 ◽  
Vol 5 (2) ◽  
pp. 363-372
Author(s):  
G N Cox ◽  
D Hirsh
Keyword(s):  
Caenorhabditis Elegans ◽  
Protein Composition ◽  
Large Family ◽  
Major Protein ◽  
Mrna Levels ◽  
Mrna Accumulation ◽  
C Elegans ◽  
Collagen Protein ◽  
Protein Components ◽  
Collagen Genes

Collagens are the major protein components of the Caenorhabditis elegans cuticle and are encoded by a large family of 40 to 150 closely related but nonidentical genes. We have determined temporal patterns of mRNA accumulation for a large number of collagen genes by screening recombinant phages and plasmids containing cloned collagen genes under high stringency conditions with 32P-labeled cDNA preparations specific for eggs or three postembryonic molts. We find that collagen mRNA levels are regulated both temporally and quantitatively during C. elegans development. Most genes studied exhibit one of four patterns of mRNA accumulation which correlate with changes in cuticle morphology and collagen protein composition during development. Our results suggest that, in general, there is a progressive activation of new collagen genes during normal development.

Protein composition of nuclear matrix preparations from HeLa cells: an immunochemical approach

1986 ◽  
Vol 80 (1) ◽  
pp. 103-122
Author(s):  
R. Verheijen ◽  
H. Kuijpers ◽  
P. Vooijs ◽  
W. van Venrooij ◽  
F. Ramaekers
Keyword(s):  
Nuclear Matrix ◽  
Connective Tissue Diseases ◽  
Protein Composition ◽  
Cytoskeletal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Core Proteins ◽  
Nuclear Rna ◽  
Hela S3 ◽  
Protein Components

Procedures for the isolation of HeLa S3 nuclear matrices were re-examined with special emphasis on the use of various nucleases and detergents as well as on the ionic strength of the final salt extraction. The protein composition of the resulting nuclear matrix preparations was analysed by one- and two-dimensional gel electrophoresis and found to be extremely reproducible. By means of co-electrophoresis several typical cytoskeletal proteins (actin, vimentin and cytokeratins) and heterogeneous nuclear RNA (hnRNA)-associated core proteins (hnRNP) were shown to be present in such nuclear matrix preparations. The nature of some other protein components was elucidated using two-dimensional immunoblotting and immunofluorescence. For this purpose mouse monoclonal antibodies to cytoskeletal components (vimentin, cytokeratins), small nuclear RNP (70 X 10(3) Mr protein of U1-RNP), hnRNP (C1/C2) and the pore-complex lamina (lamins A, B and C) were used next to human autoimmune sera obtained from patients with connective tissue diseases and directed against the residual nucleoli and the internal fibrillar mass. These antibodies enabled us to identify a number of proteins present specifically in the nuclear matrix and to show that part of the cytoskeletal proteins are still present in the isolated structures.

Sign in / Sign up

Export Citation Format

Share Document