The interaction of dansyl amino acids with bovine serum albumin

1984 ◽  
Vol 262 (4) ◽  
pp. 311-318 ◽  
Author(s):  
T. Seki ◽  
J. Komiyama ◽  
T. Iijima ◽  
U. P. Wild
Author(s):  
Yoshihiro Abe ◽  
Shikie Fukui ◽  
Yuki Koshiji ◽  
Michi Kobayashi ◽  
Tomoko Shoji ◽  
...  

2006 ◽  
Vol 18 (7) ◽  
pp. 789 ◽  
Author(s):  
Chie Suzuki ◽  
Koji Yoshioka

The effects of glutamine, hypotaurine, taurine and premixed solutions of essential amino acids (EAA) and non-essential amino acids (NEAA) on in vitro development of porcine zygotes were evaluated. The effects of refreshing the medium and replacing polyvinyl alcohol (PVA) with bovine serum albumin (BSA) on embryonic development were also investigated. Porcine zygotes produced by in vitro maturation (IVM) and in vitro fertilisation (IVF) were cultured in porcine zygote medium (PZM), as the basal culture medium, for 5 days after IVF. The total number of cells in blastocysts was significantly increased by the addition of 2 mm glutamine to PZM, as was blastocyst yields after supplementation with 0.25 to 4 mm glutamine. Addition of 1.25 to 10 mm hypotaurine to PZM significantly increased blastocyst yields. Addition of 5 mm taurine to PZM significantly increased blastocyst yield, whereas taurine had no effect on blastocyst yield in cultures already containing 5 mm hypotaurine. Adding 1× EAA significantly increased the rate of blastocyst formation compared with no or 2× EAA, whereas 2× NEAA significantly increased the total cell numbers in blastocysts compared with no NEAA. Refreshing the medium at Day 3 had no effect on blastocyst yields, whereas medium change significantly reduced the total cell numbers in blastocysts. Adjusting the amino acid concentrations of a chemically defined medium can improve the developmental competence of porcine embryo.


RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63463-63471 ◽  
Author(s):  
Mallavva B. Bolattin ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Sheshagiri R. Dixit ◽  
Shivamurti A. Chimatadar

Interactions between the BSA and CAP in the docked model. Figure showing H-bonding interactions and carisoprodol surrounded by hydrophobic amino acids Leu249, Leu250 and Gly247 in subdomain IIA.


Langmuir ◽  
2017 ◽  
Vol 33 (22) ◽  
pp. 5473-5481 ◽  
Author(s):  
Salvatore Lombardo ◽  
Samuel Eyley ◽  
Christina Schütz ◽  
Hans van Gorp ◽  
Sabine Rosenfeldt ◽  
...  

1980 ◽  
Vol 186 (3) ◽  
pp. 977-986 ◽  
Author(s):  
S A Smith ◽  
C I Pogson

1. Novel methods, using L-[ring-2-14C]tryptophan, are described for the measurement of tryptophan 2,3-dioxygenase activity and tryptophan accumulation in isolated rat liver cells. 2. The effects of bovine serum albumin, non-esterified fatty acids and neutral amino acids on tryptophan oxidation by hepatocytes and on the partition of tryptophan between free and albumin-bound forms were investigated. 3. Oxidation of physiological concentrations (0.1 mM) of tryptophan was inhibited by approx. 50% in the presence of 2% (w/v) bovine serum albumin; no effects were found at tryptophan concentrations of 0.5 mM and above. 4. Increases in free tryptophan concentrations produced by displacement of 0.1 mM-tryptophan from albumin-binding sites by palmitate resulted in increased flux through tryptophan dioxygenase. 5. Addition of a mixture of neutral amino acids, at plasma concentrations, to hepatocyte incubations had no effect on the rate of tryptophan oxidation. 6. It is concluded that alterations in free tryptophan concentrations consequent to changes in albumin binding may be an important factor in regulating tryptophan uptake and catabolism by the liver. The results are briefly discussed with reference to possible consequences on brain tryptophan metabolism.


1980 ◽  
Vol 94 (4) ◽  
pp. 571-576 ◽  
Author(s):  
Kirsti Käpyaho

Abstract. Rat ovarian ornithine decarboxylase activity could be stimulated in vitro by a variety of factors, which apparently have different modes of action. Ovarian cells prepared from pre-pubertal rats by collagenase dispersion exhibited a low but detectable ornithine decarboxylase activity after a 6-h incubation in a defined medium. The enzyme activity was markedly enhanced in vitro by hCG, which also produced increased accumulation of cyclic AMP and stimulated the secretion of progesterone. In addition to the gonadotrophin, ovarian ornithine decarboxylase activity was strikingly stimulated by some non-essential amino acids, and especially by bovine serum albumin. While markedly enhancing ornithine decarboxylase activity, none of the latter additions increased the accumulation of cyclic AMP or enhanced the secretion of progesterone. Bovine serum albumin enhanced powerfully ornithine decarboxylase activity in vitro at very small concentrations (from 0.75 μm). The half-life of the enzyme remained unchanged (26—28 min) upon stimulation indicating that the stimulation mechanism did not involve any stabilization of the enzyme.


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