Identification of the corticotropin binding domain of bovine serum albumin by photoaffinity labeling

Biochemistry ◽  
1981 ◽  
Vol 20 (12) ◽  
pp. 3380-3385 ◽  
Author(s):  
Koji Muramoto ◽  
J. Ramachandran
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Photoaffinity Labeling ◽  
Binding Domain

Stereoselective oxidation of aromatic sulfides and sulfoxides in the binding domain of bovine serum albumin

1981 ◽  
Vol 10 (3) ◽  
pp. 311-323 ◽  
Author(s):  
Toyonari Sugimoto ◽  
Toshio Kokubo ◽  
Jinsei Miyazaki ◽  
Shigeo Tanimoto ◽  
Masaya Okano
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Domain ◽  
Stereoselective Oxidation

Asymmetric reduction of alkyl aryl ketones in the binding domain of bovine serum albumin

1981 ◽  
Vol 10 (1) ◽  
pp. 104-113 ◽  
Author(s):  
Toyonari Sugimoto ◽  
Toshio Kokubo ◽  
Yasuo Matsumura ◽  
Jinsei Miyazaki ◽  
Shigeo Tanimoto ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Asymmetric Reduction ◽  
Binding Domain ◽  
Alkyl Aryl ◽  
Aryl Ketones

scholarly journals RESPONS PERTUMBUHAN DAN EKSPRESI GEN UDANG VANAME, Litopenaeus vannamei SETELAH DIRENDAM DALAM LARUTAN HORMON PERTUMBUHAN REKOMBINAN IKAN KERAPU KERTANG

2012 ◽  
Vol 7 (3) ◽  
pp. 359
Author(s):  
Siti Subaidah ◽  
Odang Carman ◽  
Komar Sumantadinata ◽  
Sukenda Sukenda ◽  
Alimuddin Alimuddin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Litopenaeus Vannamei ◽  
Bovine Serum ◽  
Insulin Binding ◽  
Binding Domain ◽  
Realtime Pcr

Pertumbuhan ikan dapat ditingkatkan menggunakan hormon pertumbuhan rekombinan. Penelitian ini bertujuan mengkaji respons pertumbuhan dan ekspresi gen udang vaname, Litopenaeus vannamei setelah direndam dengan hormon pertumbuhan rekombinan ikan kerapu kertang, Epinephelus lanceolatus (rElGH). Pada percobaan pertama, post larva stadia 2 (PL-2) sebanyak 1.500 ekor direndam selama 1 jam dalam 1 liter air laut yang mengandung rElGH lima dosis berbeda, yaitu 150; 15; 1,5; 0,15; dan 0,015 mg/L dan bovine serum albumin 0,01%. Setiap perlakuan diulang 3 kali. Perendaman dilakukan dalam kantong plastik ditambah oksigen (volume air :oksigen = 1:5). Udang dipelihara dalam akuarium volume 60 liter dengan kepadatan 25 ekor/litersampai PL-14. Hasil penelitian menunjukkan bahwa dosis 15 mg/L memberikan peningkatan bobot badan, panjang badan, dan sintasan tertinggi (P<0,05) masing-masing sebesar 37,77%; 12,75%; dan 9,45% dibandingkan dengan kontrol. Ekspresi mRNA single insulin binding domain (SIBD) pada PL-14 yang dianalisis dengan realtime PCR menunjukkan kenaikan sebesar 3,3 kali pada udang yang direndam rElGH dibandingkan dengan kontrol, dan dapat dinyatakan bahwa SIBD berperan penting dalam induksi pertumbuhan. Tingkat ekspresi moult inhibiting hormone meningkat sekitar 13%, sedangkan ekspresi cyclopilin A pada udang yang direndam rElGH sama dengan kontrol. Pada percobaan kedua, perendaman PL-2 dalam larutan rElGH dosis 15 mg/L dengan lama waktu 3 jam meningkatkan bobot badan sebesar 62,18% lebih tinggi daripada perendaman 1 jam. Dengan demikian, perendaman udang dalam larutan rElGH meningkatkan pertumbuhan dan ekspresi gen SIBD, dan metode ini dapat berguna dalam peningkatan produksi budidaya. 

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

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