A comparison of soluble-protein fractions in two acanthocephalan genera

1974 ◽  
Vol 52 (7) ◽  
pp. 823-825 ◽  
Author(s):  
Eldon S. Eveleigh

Micro-starch gel electrophoretic separation of soluble proteins from whole-Acanthocephala homogenates yielded band profiles useful for distinguishing between the genera Prosthorhynchus and Polymorphus. Certain protein bands were common to both genera while other bands were characteristic. Band patterns for two stages of Polymorphus were identical except for differences in the relative concentration of certain bands.

1991 ◽  
Vol 24 (4) ◽  
pp. 235-243 ◽  
Author(s):  
Eridan M. Coutinho ◽  
Frederico G. C. Abath ◽  
Lucila P. C. G. de Freitas ◽  
Aureni C. Salzano ◽  
Maria A. Lapa ◽  
...  

Body, liver and spleen weights; histopathology of the liver, spleen and intestines; hepatic and serum soluble proteins changes were the parameters studied in undernourished Swiss albino mice experimentally infected with S. mansoni. Non-infected deficient animab had lower liver/body weight and spleen/body weight ratios as compared to the controls (22.60% casein group). Infected mice showed higher values regardless the type of diet. Undernourished infected subgroup showed a persistent exudative periovular reaction in the liver. Soluble hepatic proteins content and serum protein fractions appeared to be lower in the deficient infected mice. A significant difference was detected in the gammaglobulin fraction between infected and non-infected animals fed the control diet with higher values for the former. Our data suggest that the effects of malnutrition, per se, are sometimes more detrimental to the host than those due to Manson 's schistosomiasis.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Zhongqi He ◽  
Christopher P. Mattison ◽  
Dunhua Zhang ◽  
Casey C. Grimm

AbstractIn this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.


PROTEOMICS ◽  
2011 ◽  
Vol 11 (21) ◽  
pp. 4274-4278 ◽  
Author(s):  
Xiaoqiang Qiao ◽  
Dingyin Tao ◽  
Yanyan Qu ◽  
Liangliang Sun ◽  
Liang Gao ◽  
...  

2012 ◽  
Vol 13 (3) ◽  
pp. 256
Author(s):  
Dyah Koesoemawardani ◽  
Fibra Nurainy ◽  
Sri Hidayati

This study aimed to find optimum manufacturing trash fish protein hydrolyzate using the commercial papainenzyme. It is known that fish protein hydrolysates have good functional properties, so it is more widely utilized,especially for food. The study was conducted in two stages, the first stage was to make trash fish protein hydrolyzatetreated with enzyme concentration of 3%, 5%, 7% (w/w), and pH 5; 5.5; 6; 6.5; 7, whereas second stage was to maketrash fish protein hydrolyzate with same from the first stage and so the best treatment followed by treatment ofhalf-hour long incubation and one hour. Parameters observed were soluble protein, foamability, fat binding capacityand emulsion stability. The treatment was repeated three times and the first phase of data analysis using advancedtesting LSD and the second stage using the T test. Results show that the best soluble protein to produce a trashfish protein hydrolyzate enzyme was at a concentration of 5% and pH = 6.5 that was equal to 19.71%. In half an hourincubation produce higher soluble protein values and foamability that were equal to 24.97% and 9.63%, while thebinding capacity of fat in one hour incubation produces a higher value that was equal to 5.03%. Meanwhile, emulsionstability did not differ significantly at both incubation time.


1968 ◽  
Vol 14 (11) ◽  
pp. 1169-1172 ◽  
Author(s):  
Awatar S. Sekhon ◽  
Nicholas Colotelo

Changes in dry weight, hydrogen cyanide production, peroxidase, and soluble proteins of mycelium of a low-temperature basidiomycete with age of cultures were studied.Hydrogen cyanide was detected only after there was a decrease in growth of mycelium as determined by dry-weight measurements. Polyacrylamide gel electrophoretic analyses showed that the pattern and numbers of peroxidase and other soluble-protein bands varied with the age of the culture. Concomitant with decreases in yield of mycelium, there was a decrease in the numbers of peroxidase and soluble-protein bands.


1965 ◽  
Vol 43 (4) ◽  
pp. 593-602 ◽  
Author(s):  
E. H. Salkeld

The soluble or lyo- esterases from the developing embryo and the young nymph of the large milkweed bug, Oncopeltus fasciatus (Dallas), have been separated by a starch gel electrophoretic method. With the substrate α-naphthyl acetate, 14 bands of esterase activity occurred in the 2-day-old egg and this number increased to 19 in the 1-day-otd nymph. Variation in the intensity of esterase activity also occurred during development; the activity of some esterases increased while that of others decreased. An attempt was made to classify the separated enzymes as cholinesterases, aliesterases, and aromatic esterases according to their reactions to certain carbamate and organophosphate inhibitors. When these criteria were used, no cholinesterase was found and two of the bands of esterase activity did not react as either aliesterase or aromatic esterase.


1990 ◽  
Vol 36 (1) ◽  
pp. 1-5 ◽  
Author(s):  
T. E. Cleveland ◽  
D. Bhatnagar

The accumulation of both activity and protein of a methyltransferase (MTase) from Aspergillus parasiticus, which catalyzes conversion of sterigmatocystin to O-methylsterigmatocystin in the aflatoxin pathway, was detected in fungal mycelia slightly before the onset of aflatoxin biosynthesis in the same cultures. MTase protein was identified in mycelial postmicrosomal (soluble protein) fractions by electrophoresis and subsequent immunoblotting using antiserum raised against purified MTase protein; MTase activity was determined by measuring the rate of conversion of sterigmatocystin to O-methylsterigmatocystin in the presence of soluble protein fractions. Using the above technique, it was determined that MTase protein as well as MTase activity increased sharply in mycelia 30 to 45 h after inoculation, shortly after which, mycelial growth rate began to decline. During the subsequent time interval (45 to 70 h after inoculation), a sharp increase in aflatoxin levels was detected in the culture medium. Results obtained from an experiment in which cycloheximide was added to cultures at various times to inhibit protein synthesis and from an experiment in which mycelial proteins were radiolabelled to identify newly synthesized proteins indicated that accumulation of MTase activity and protein in late growth phase mycelia is due to de novo protein synthesis. Key words: aflatoxin, methyltransferase, biosynthetic pathway.


PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e30746 ◽  
Author(s):  
Shraddha Kumari ◽  
Pragya Misra ◽  
Rati Tandon ◽  
Mukesh Samant ◽  
Shyam Sundar ◽  
...  

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