Heterogeneity of the ciliary epithelium of the rat eye as revealed by spot 35 protein (a Purkinje cell specific protein)-like immunoreactivity

1988 ◽  
Vol 89 (1) ◽  
pp. 53-56 ◽  
Author(s):  
H. Kondo ◽  
M. Yamamoto ◽  
T. Yamakuni ◽  
Y. Takahashi
Keyword(s):  
Purkinje Cell ◽  
Protein A ◽  
Specific Protein ◽  
Ciliary Epithelium

Involvement of spot 35 protein, a cerebellar protein, in modulation of Purkinje cell activity of the rat cerebellum

1985 ◽  
Vol 108 (3) ◽  
pp. 309-313 ◽  
Author(s):  
Shoji Maruyama ◽  
Ge Zhang ◽  
Yoshimatsu Tamura ◽  
Tohru Yamakuni ◽  
Yasuo Takahashi
Keyword(s):  
Purkinje Cell ◽  
Protein A ◽  
Cell Activity ◽  
Rat Cerebellum

scholarly journals Development of QCM Biosensor with Specific Cow Milk Protein Antibody for Candidate Milk Adulteration Detection

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Setyawan P. Sakti ◽  
Nur Chabibah ◽  
Senja P. Ayu ◽  
Masdiana C. Padaga ◽  
Aulanni’am Aulanni’am
Keyword(s):  
Milk Protein ◽  
Protein A ◽  
Goat Milk ◽  
Specific Protein ◽  
Cow Milk ◽  
Frequency Change ◽  
Milk Product ◽  
Reaction Cell ◽  
Buffer Solution ◽  
Milk Adulteration

Adulteration of goat milk is usually done using cow’s milk product. Cow milk is used as it is widely available and its price is cheaper compared to goat milk. This paper shows a development of candidate tools for milk adulteration using cow milk. A quartz crystal microbalance immunosensor was developed using commercial crystal resonator and polyclonal antibody specific to cow milk protein. A specific protein at 208 KDa is found only in cow milk and does not exist in goat milk. The existence of this protein can be used as an indicator of cow milk content in a target solution. To detect the PSS 208 kDa protein, antibody specific to the PSS 208 was developed. The purified antibody was immobilized on top of the sensor surface on a polystyrene layer. The fraction of the immobilized antibody on the sensor was found at 1.5% of the given antibody. Using a static reaction cell, the developed immunosensor could detect the specific cow milk protein in buffer solution. The detection limit is 1 ppm. A linear relationship between frequency change and specific protein of cow milk concentration is found from a concentration of 1 ppm to 120 ppm.

Production of Brucella abortus-specific protein A-reactive antibodies (IgG2) in infected and vaccinated cattle

1986 ◽  
Vol 12 (1) ◽  
pp. 43-53 ◽  
Author(s):  
Michael J.P. Lawman ◽  
David R. Ball ◽  
Edward M. Hoffmann ◽  
Lucy E. Desjardin ◽  
Michael D.P. Boyle
Keyword(s):  
Brucella Abortus ◽  
Protein A ◽  
Specific Protein

Biochemical and Immunological Studies on the P400 Protein, a Protein Characteristic of the Purkinje Cell from Mouse and Rat Cerebellum

1979 ◽  
Vol 2 (6) ◽  
pp. 254-275 ◽  
Author(s):  
Katsuhiko Mikoshiba ◽  
Monique Huchet ◽  
Jean-Pierre Changeux
Keyword(s):  
Purkinje Cell ◽  
Protein A ◽  
Rat Cerebellum

scholarly journals Oestrogen-induced synthesis of thiamin-binding protein in immature chicks. Kinetics of induction, hormonal specificity and modulation

1980 ◽  
Vol 186 (1) ◽  
pp. 201-210 ◽  
Author(s):  
Kalappagowda Muniyappa ◽  
P. Radhakantha Adiga
Keyword(s):  
Half Life ◽  
Binding Proteins ◽  
Binding Protein ◽  
Steroid Hormone ◽  
Plasma Concentrations ◽  
Protein A ◽  
Specific Protein ◽  
Clear Cut ◽  
Apparent Similarity ◽  
Kinetics Of

A specific radioimmunoassay procedure was developed to monitor the plasma concentrations of thiamin-binding protein, a minor yolk constituent of the chicken egg. By using this sensitive assay, the kinetics of oestrogen-induced elaboration of this specific protein in immature chicks was investigated. After a single injection of the steroid hormone, with an initial lag period of 4–5h the thiamin-binding protein rapidly accumulated in the plasma, attaining peak concentrations around 75h and declining thereafter. A 4-fold amplification of the response was noticed during the secondary stimulation, and this increased to 9-fold during the tertiary stimulation with the steroid hormone. The magnitude of the response was dependent on the hormone dose, and the initial latent period and the duration of the ascending phase of induction were unchanged for the hormonal doses tested during both the primary and secondary stimulations. The circulatory half-life of the protein was 6h as calculated from the measurement of the rate of disappearance of the exogenously administered 125I-labelled protein. Simultaneous administration of progesterone, dihydrotestosterone or corticosterone did not alter the pattern of induction. On the other hand, hyperthyroidism markedly decreased the oestrogenic response, whereas propylthiouracil-induced hypothyroidism had the opposite effect. The anti-oestrogen E- and Z-clomiphene citrates, administered 30min before oestrogen, effectively blocked the hormonal induction. α-Amanitin and cycloheximide administered along with or shortly after the sex steroid severely curtailed the protein elaboration. A comparison of the kinetics of induction of thiamin- and riboflavin-binding proteins by oestrogen revealed that, beneath an apparent similarity, a clear-cut difference exists between the two vitamin-binding proteins, particularly with regard to hormonal dose-dependent sensitivity of induction and the half-life in circulation. The steroid-mediated elaboration of the two yolk proteins thus appears to be not strictly co-ordinated, despite several common regulatory features underlying their induction.

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