Oestradiol-17β induces the major vitelline envelope proteins in both sexes in teleosts

1991 ◽  
Vol 131 (2) ◽  
pp. 229-236 ◽  
Author(s):  
S. J. Hyllner ◽  
D. O. Oppen-Berntsen ◽  
J. V. Helvik ◽  
B. T. Walther ◽  
C. Haux
Keyword(s):  
Rainbow Trout ◽  
Amino Acid ◽  
Brown Trout ◽  
Polyclonal Antibodies ◽  
Ovarian Follicle ◽  
Envelope Proteins ◽  
Structural Proteins ◽  
Males And Females ◽  
Vitelline Envelope ◽  
Separate Class

ABSTRACT During growth of the ovarian follicle, the teleost oocyte becomes surrounded by an acellular coat, the vitelline envelope. The nature, origin and number of the vitelline envelope proteins in fish appear to vary with species. In this work, polyclonal antibodies directed against vitelline envelope proteins from rainbow trout, brown trout and turbot were used to show that oestradiol-17β induces the major vitelline envelope proteins in juveniles, both males and females, from different species. The fact that males can synthesize vitelline envelope constituents shows that the origin of these proteins is not confined to the ovary. The vitelline envelope of rainbow trout eggs consists of three major proteins, designated α (60 kDa), β (55 kDa) and γ (50 kDa). The amino acid composition of each of the three proteins indicated that the three proteins are alike and the suggestion that these proteins represent a separate class of structural proteins is sustained. Journal of Endocrinology (1991) 131, 229–236

Immunochemical detection of the major vitelline envelope proteins in the plasma and oocytes of the maturing female rainbow trout, Oncorhynchus mykiss

1992 ◽  
Vol 135 (2) ◽  
pp. 303-NP ◽  
Author(s):  
S. J. Hyllner ◽  
C. Haux
Keyword(s):  
Rainbow Trout ◽  
Total Body Weight ◽  
Envelope Proteins ◽  
Major Protein ◽  
Endocrine Control ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Blot Technique ◽  
Immunochemical Detection ◽  
Vitelline Envelope ◽  
Total Body

ABSTRACT The major vitelline envelope proteins were detected in the plasma of female rainbow trout maturing under natural conditions by using the Western blot technique. Females were sampled every month from July until ovulation in January. The amount of vitelline envelope proteins in plasma increased markedly as the gonads increased in size from 0·4 to about 15% of the total body weight. The plasma level of oestradiol-17β largely followed the alterations in the amount of vitelline envelope proteins, indicating the endocrine control of vitelline envelope protein synthesis. In addition, plasma vitellogenin changed in a manner that resembled the changes in the amount of plasma vitelline envelope proteins. The appearance and growth of the vitelline envelope during oocyte development was demonstrated using immunohistochemical methods. The vitelline envelopes from oocytes at different stages of development were immunoreactive with the antibodies directed against the major vitelline envelope proteins. No immunoreactivity could be observed in the ooplasm or in the surrounding follicular cells, which indicated that the major vitelline envelope proteins were of extraovarian origin. The present study further supports the hypothesis that the major protein constituents of the vitelline envelope in teleosts are under the endocrine control of oestradiol17β and that the site of synthesis is outside the ovary. Journal of Endocrinology (1992) 135, 303–309

scholarly journals Mass Spectrometric Evidence That Proteolytic Processing of Rainbow Trout Egg Vitelline Envelope Proteins Takes Place on the Egg

2005 ◽  
Vol 280 (45) ◽  
pp. 37585-37598 ◽  
Author(s):  
Costel C. Darie ◽  
Martin L. Biniossek ◽  
Mary A. Gawinowicz ◽  
Yelena Milgrom ◽  
Joerg O. Thumfart ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Envelope Proteins ◽  
Mass Spectrometric ◽  
Proteolytic Processing ◽  
Mass Spectrometric Evidence ◽  
Vitelline Envelope

scholarly journals Putative imbalanced amino acid metabolism in rainbow trout long term fed a plant-based diet as revealed by 1H-NMR metabolomics

2021 ◽  
Vol 10 ◽  
Author(s):  
Catherine Deborde ◽  
Blandine Madji Hounoum ◽  
Annick Moing ◽  
Mickaël Maucourt ◽  
Daniel Jacob ◽  
...  
Keyword(s):  
Amino Acids ◽  
Rainbow Trout ◽  
Amino Acid ◽  
Amino Acid Content ◽  
Proton Nuclear Magnetic Resonance ◽  
Free Form ◽  
Metabolomic Analysis ◽  
Nmr Metabolomics ◽  
H Nmr

Abstract The long-term effect of a plant (P)-based diet was assessed by proton nuclear magnetic resonance (1H-NMR) metabolomics in rainbow trout fed a marine fish meal (FM)–fish oil (FO) diet (M), a P-based diet and a control commercial-like diet (C) starting with the first feeding. Growth performances were not heavily altered by long-term feeding on the P-based diet. An 1H-NMR metabolomic analysis of the feed revealed significantly different soluble chemical compound profiles between the diets. A set of soluble chemical compounds was found to be specific either to the P-based diet or to the M diet. Pterin, a biomarker of plant feedstuffs, was identified both in the P-based diet and in the plasma of fish fed the P-based diet. 1H-NMR metabolomic analysis on fish plasma and liver and muscle tissues at 6 and 48 h post feeding revealed significantly different profiles between the P-based diet and the M diet, while the C diet showed intermediate results. A higher amino acid content was found in the plasma of fish fed the P-based diet compared with the M diet after 48 h, suggesting either a delayed delivery of the amino acids or a lower amino acid utilisation in the P-based diet. This was associated with an accumulation of essential amino acids and the depletion of glutamine in the muscle, together with an accumulation of choline in the liver. Combined with an anticipated absorption of methionine and lysine supplemented in free form, the present results suggest an imbalanced essential amino acid supply for protein metabolism in the muscle and for specific functions of the liver.

Variation within and between Rivers in Adult Size and Sea Age at Maturity of Anadromous Brown Trout, Salmo trutta

1991 ◽  
Vol 48 (6) ◽  
pp. 1015-1021 ◽  
Author(s):  
Jan Henning L'Abée-Lund
Keyword(s):  
Brown Trout ◽  
Sexual Maturity ◽  
Salmo Trutta ◽  
Adult Size ◽  
Age At Maturity ◽  
Migration Distance ◽  
Spawning Area ◽  
Brown Trout Salmo Trutta ◽  
Males And Females ◽  
The Mean

I compared adult size and sea age at sexual maturity among nine populations of anadromous brown trout, Salmo trutta, in two Norwegian rivers to determine the extent of inter- and intrariverine variations. Variation in the mean length of spawners and in the mean sea age at sexual maturity were mainly dependent on the variations found within rather than between rivers. Mean lengths and mean age at maturity of males increased significantly with increasing altitude of the spawning area and with migration distance in freshwater. In females, positive significant correlations were found with mean lengths and altitude of the spawning area and with mean sea age at maturity and both spawning site altitude and migration distance. Mean lengths and ages of males and females were not significantly correlated with the rate of water discharge in the streams during spawning. The size of gravel substrate for spawning was of minor importance in explaining interpopulation variation in mean female size. The increase noted in mean length and in mean sea age at maturity of both males and females is probably an adaptation to greater energy expenditure to reach the uppermost natal spawning areas.

scholarly journals Streptococcus salivarius Fimbriae Are Composed of a Glycoprotein Containing a Repeated Motif Assembled into a Filamentous Nondissociable Structure

2001 ◽  
Vol 183 (9) ◽  
pp. 2724-2732 ◽  
Author(s):  
Céline Lévesque ◽  
Christian Vadeboncoeur ◽  
Fatiha Chandad ◽  
Michel Frenette
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cell Surface ◽  
Polyclonal Antibodies ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Spontaneous Mutant ◽  
Streptococcus Salivarius ◽  
Streptococcal Species ◽  
Repeated Motif

ABSTRACT Streptococcus salivarius, a gram-positive bacterium found in the human oral cavity, expresses flexible peritrichous fimbriae. In this paper, we report purification and partial characterization of S. salivarius fimbriae. Fimbriae were extracted by shearing the cell surface of hyperfimbriated mutant A37 (a spontaneous mutant of S. salivarius ATCC 25975) with glass beads. Preliminary experiments showed that S. salivariusfimbriae did not dissociate when they were incubated at 100°C in the presence of sodium dodecyl sulfate. This characteristic was used to separate them from other cell surface components by successive gel filtration chromatography procedures. Fimbriae with molecular masses ranging from 20 × 106 to 40 × 106Da were purified. Examination of purified fimbriae by electron microscopy revealed the presence of filamentous structures up to 1 μm long and 3 to 4 nm in diameter. Biochemical studies of purified fimbriae and an amino acid sequence analysis of a fimbrial internal peptide revealed that S. salivarius fimbriae were composed of a glycoprotein assembled into a filamentous structure resistant to dissociation. The internal amino acid sequence was composed of a repeated motif of two amino acids alternating with two modified residues: A/X/T-E-Q-M/φ, where X represents a modified amino acid residue and φ represents a blank cycle. Immunolocalization experiments also revealed that the fimbriae were associated with a wheat germ agglutinin-reactive carbohydrate. Immunolabeling experiments with antifimbria polyclonal antibodies showed that antigenically related fimbria-like structures were expressed in two other human oral streptococcal species, Streptococcus mitis andStreptococcus constellatus.

Monoclonal and Polyclonal Antibodies Against the HCV Envelope Proteins

2009 ◽  
Vol 13 (3) ◽  
pp. 477-486 ◽  
Author(s):  
Heshaam M. Mir ◽  
Aybike Birerdinc ◽  
Zobair M. Younossi
Keyword(s):  
Polyclonal Antibodies ◽  
Envelope Proteins

Amino acid content of Baltic herring and rainbow trout roe

1980 ◽  
Vol 28 (5) ◽  
pp. 908-911 ◽  
Author(s):  
Jukka K. Kaitaranta ◽  
Raila Lamppu ◽  
Reino R. Linko
Keyword(s):  
Rainbow Trout ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Baltic Herring
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