Practical procedure for enzyme immunoassay of progesterone in bovine serum

1980 ◽  
Vol 93 (2) ◽  
pp. 223-227 ◽  
Author(s):  
Toshihiko Nakao
Keyword(s):  
Enzyme Immunoassay ◽  
Bovine Serum ◽  
Rabbit Antiserum ◽  
Water Soluble ◽  
Serum Progesterone ◽  
E Coli ◽  
Practical Procedure ◽  
Detectable Concentration ◽  
Rate Correlation ◽  
Hydrolysis Of

Abstract. An enzyme immunoassay of progesterone was established by using β-galactosidase from E. coli as a label. The enzyme was conjugated with 11α-hydroxyprogesterone-hemisuccinate using water-soluble carbodiimide. Rabbit antiserum to 11α-hydroxyprogesterone-hemisuccinate-bovine serum albumin was previously obtained and anti-rabbit gamma globulin goat serum was used as second antibody. The enzyme activity was measured by utilizing hydrolysis of O-nitrophenyl-β-D-galactopyranoside. The least detectable concentration of progesterone was 12 pg per tube. The measurable range of progesterone in 0.1 ml of bovine serum was between 0.25 ng/ml and 10 ng/ml. This method satisfied the general criteria regarding specifity, precision and recovery rate. Correlation between the progesterone levels determined by enzyme immunoassay and radioimmunoassay was quite high (r = 0.99, P ≦ 0.01). The present enzyme immunoassay can be applied for practical and routine analysis of serum progesterone.

Sensitive Enzyme Immunoassay of Cephalexin Residues in Milk, Hen Tissues, and Eggs

1988 ◽  
Vol 71 (5) ◽  
pp. 915-920
Author(s):  
Tsunehiro Kitagawa ◽  
Yukio Gotoh ◽  
Kazuyo Uchihara ◽  
Youko Kohri ◽  
Tihoko Kinoue ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Enzyme Immunoassay ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Rabbit Antiserum ◽  
Egg Yolk ◽  
Amino Group ◽  
Thiol Groups ◽  
Cross Linker

Abstract A sensitive enzyme immunoassay for cephalexin (CEX) was developed using the rabbit antiserum to CEX, Β-D-galactosidase-labeled CEX, and a double-antibody separation method. The immunogen of CEX was prepared by coupling the amino group of CEX to thiol groups introduced into bovine serum albumin by the use of N-(mmaleimidobenzoyloxy) succinimide as a cross-linker. Highly titered antiserum to CEX was produced in rabbits immunized with the immunogen. Enzyme labeling of CEX with Β-D-galactosidase was done by using 7V-(gamma-maleimidobutyryloxy)succinimide as the crosslinker. The limit of detection was 30 ng CEX/mL sample solution. Application of the method to CEX drug residues detected 30 ng/mL in milk, 60 ng/g in egg yolk, and 400 ng/g in hen tissue.

scholarly journals Reclamation of Marine Chitinous Materials for Chitosanase Production via Microbial Conversion by Paenibacillus macerans

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 429 ◽  
Author(s):  
Chien Doan ◽  
Thi Tran ◽  
Van Nguyen ◽  
Anh Nguyen ◽  
San-Lang Wang
Keyword(s):  
Water Soluble ◽  
Microbial Conversion ◽  
E Coli ◽  
Molecular Weights ◽  
Chitosan Oligosaccharides ◽  
Agricultural Applications ◽  
Paenibacillus Macerans ◽  
Shrimp Heads ◽  
Chitinous Materials ◽  
Hydrolysis Of

Chitinous materials from marine byproducts elicit great interest among biotechnologists for their potential biomedical or agricultural applications. In this study, four kinds of marine chitinous materials (squid pens, shrimp heads, demineralized shrimp shells, and demineralized crab shells) were used to screen the best source for producing chitosanase by Paenibacillus macerans TKU029. Among them, the chitosanase activity was found to be highest in the culture using the medium containing squid pens as the sole carbon/nitrogen (C/N) source. A chitosanase which showed molecular weights at 63 kDa was isolated from P. macerans cultured on a squid pens medium. The purified TKU029 chitosanase exhibited optimum activity at 60 °C and pH 7, and was stable at temperatures under 50 °C and pH 3-8. An analysis by MALDI-TOF MS revealed that the chitosan oligosaccharides (COS) obtained from the hydrolysis of water-soluble chitosan by TKU029 crude enzyme showed various degrees of polymerization (DP), varying from 3–6. The obtained COS enhanced the growth of four lactic acid bacteria strains but exhibited no effect on the growth of E. coli. By specialized growth enhancing effects, the COS produced from hydrolyzing water soluble chitosan with TKU029 chitinolytic enzymes could have potential for use in medicine or nutraceuticals.

scholarly journals Optimizing Chitin Depolymerization by Lysozyme to Long-Chain Oligosaccharides

Marine Drugs ◽  
2021 ◽  
Vol 19 (6) ◽  
pp. 320
Author(s):  
Arnaud Masselin ◽  
Antoine Rousseau ◽  
Stéphanie Pradeau ◽  
Laure Fort ◽  
Rodolphe Gueret ◽  
...  
Keyword(s):  
Time Course ◽  
Water Soluble ◽  
Organic Fertilizers ◽  
Symbiotic Associations ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Ecological Transition ◽  
Optimized Conditions ◽  
Hydrolysis Of ◽  
Long Chain

Chitin oligosaccharides (COs) hold high promise as organic fertilizers in the ongoing agro-ecological transition. Short- and long-chain COs can contribute to the establishment of symbiotic associations between plants and microorganisms, facilitating the uptake of soil nutrients by host plants. Long-chain COs trigger plant innate immunity. A fine investigation of these different signaling pathways requires improving the access to high-purity COs. Here, we used the response surface methodology to optimize the production of COs by enzymatic hydrolysis of water-soluble chitin (WSC) with hen egg-white lysozyme. The influence of WSC concentration, its acetylation degree, and the reaction time course were modelled using a Box–Behnken design. Under optimized conditions, water-soluble COs up to the nonasaccharide were formed in 51% yield and purified to homogeneity. This straightforward approach opens new avenues to determine the complex roles of COs in plants.

Transfecting pDNA to E . coli DH5α using bovine serum albumin nanoparticles as a delivery vehicle

Luminescence ◽  
2014 ◽  
Vol 30 (5) ◽  
pp. 583-591 ◽  
Author(s):  
Jitendra Wagh ◽  
Kuldeep J. Patel ◽  
Parth Soni ◽  
Krutika Desai ◽  
Pratik Upadhyay ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Delivery Vehicle ◽  
E Coli ◽  
Albumin Nanoparticles

Inhibition of ATPase activity of E. coli F1 by the water-soluble carbodiimide EDC is due to modification of several carboxyls in the .beta. subunit

Biochemistry ◽  
1984 ◽  
Vol 23 (18) ◽  
pp. 4134-4140 ◽  
Author(s):  
Hans Ruedi Lotscher ◽  
Catherina DeJong ◽  
Roderick A. Capaldi
Keyword(s):  
Atpase Activity ◽  
Water Soluble ◽  
Beta Subunit ◽  
E Coli

THE WATER-SOLUBLE POLYSACCHARIDES OF DERMATOPHYTES: IV. GALACTOMANNANS I FROM TRICHOPHYTON GRANULOSUM, TRICHOPHYTON INTERDIGITALE, MICROSPORUM QUINCKEANUM, TRICHOPHYTON RUBRUM, AND TRICHOPHYTON SCHÖNLEINII

1965 ◽  
Vol 43 (1) ◽  
pp. 30-39 ◽  
Author(s):  
C. T. Bishop ◽  
M. B. Perry ◽  
F. Blank ◽  
F. P. Cooper
Keyword(s):  
Aqueous Solutions ◽  
Copper Complexes ◽  
Trichophyton Rubrum ◽  
Periodate Oxidation ◽  
Structural Features ◽  
Water Soluble ◽  
Major Constituent ◽  
Branch Points ◽  
Terminal Units ◽  
Hydrolysis Of

A group of polysaccharides, called galactomannans I, were precipitated as their insoluble copper complexes from aqueous solutions of the crude polysaccharides obtained from each of the organisms designated in the title. The five galactomannans I were homogeneous under conditions of electrophoresis and ultracentrifugation and had high positive specific rotations. The major constituent monosaccharide was D-mannose; amounts of D-galactose ranged from nil for the polysaccharide from T. rubrum to 13% for that from T. schönleinii. Methylation and hydrolysis of the five galactomannans I yielded varying amounts of the following: 2,3,5,6-tetra-O-methyl-D-galactose (not present in the products from T. rubrum), 2,3,4,6-tetra-O-methyl-D-mannose, 2,3,4-tri-O-methyl-D-mannose, 2,4,6-tri-O-methyl-D-mannose, 3,4-di-O-methyl-D-mannose, and 3,5-di-O-methyl-D-mannose. Periodate oxidation results agreed with the methylation studies. The gross structural features of each galactomannan I appear to be the same, namely, a basic chain of 1 → 6 linked α-D-mannopyranose units for approximately every 22 of which there is a 1 → 3 linked α-D-mannopyranose residue. Branch points occur along the 1 → 6 linked chain at the C2 positions of the D-mannopyranose units and once in every 45 units at the C2 position of a 1 → 6 linked D-mannofuranose residue. The D-galactose in the polysaccharides is present exclusively as non-reducing terminal furanose units; non-reducing terminal units of D-mannopyranose are also present. The variations in the identities and relative amounts of the non-reducing terminal units were the only apparent differences in the gross structural features within this group of polysaccharides.

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