scholarly journals The Amino Acid Sequence and Copper(II)-binding Properties of Peptide (1–24) of Bovine Serum Albumin

1967 ◽  
Vol 242 (23) ◽  
pp. 5451-5459 ◽  
Author(s):  
William T. Shearer ◽  
Ralph A. Bradshaw ◽  
Frank R.N. Gurd ◽  
Peters Theodore
2021 ◽  
Author(s):  
Olesya Viktorovna Pokidova ◽  
◽  
Nina Sergeevna Emel’yanova ◽  
Alexander Vasilievich Kulikov ◽  
Alexander Ivanovich Kotelnikov ◽  
...  

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.


1972 ◽  
Vol 50 (5) ◽  
pp. 563-573 ◽  
Author(s):  
Stephen J. Wetmore ◽  
Jacob A. Verpoorte

Two distinct fractions showing both β-N-acetyl-D-glucosaminidase (EC 3.2.1.30) and β-N-acetyl-D-galactosaminidase activity were isolated and purified from pig kidney. These preparations, which were designated A and B, were not stable during gel chromatography or prolonged dialysis. Final purifications of 600-fold for enzyme A and 440-fold for enzyme B were obtained.Gel electrophoresis and ultracentrifugation studies indicated heterogeneity in both preparations. The amino acid compositions of both preparations were very similar. Ultracentrifugation studies suggested the formation of subunits in the presence of 5 M guanidine–HCl and 1 mM dithiothreitol.A study of the enzymatic properties also showed great similarities between the two enzyme forms. Both enzymes had identical Michaelis–Menten constants of 1.88 mM for p-nitrophenyl-β-N-acetyl-D-glucosaminide and 0.38 mM for p-nitrophenyl-β-N-acetyl-D-galactosaminide. Although bovine serum albumin enhanced the activity of the enzymes it did not change the Km values. The pH-rate profiles of both enzymes with the substrate p-nitrophenyl-β-N-acetyl-D-glucosaminide showed two peaks. When p-nitrophenyl-β-N-acetyl-D-galactosaminide was used as substrate, only one peak was observed in the pH–rate profiles. However, in this case a distinct shoulder could be detected in these peaks. Heating at 50° destroyed the activities of both forms of the enzyme rapidly, but addition of bovine serum albumin protected against heat inactivation.


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.


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