scholarly journals Effects of Bivalent Metal Cations on the Conformation and Aggregation of Poly(L-glutamic acid)

1986 ◽  
Vol 59 (2) ◽  
pp. 587-591 ◽  
Author(s):  
Hiroshi Maeda ◽  
Tsuyoshi Hiramatsu ◽  
Shoichi Ikeda
Keyword(s):  
Glutamic Acid ◽  
Metal Cations ◽  
Bivalent Metal

Complexes of bivalent metal cations in electrospray mass spectra of common organic compounds

2002 ◽  
Vol 37 (6) ◽  
pp. 617-622 ◽  
Author(s):  
Tomasz Bie?kowski ◽  
Agnieszka Brodzik-Bie?kowska ◽  
Witold Danikiewicz
Keyword(s):  
Organic Compounds ◽  
Mass Spectra ◽  
Metal Cations ◽  
Bivalent Metal

scholarly journals Preparation and general properties of a soluble adenosine triphosphatase from mitochondria

1967 ◽  
Vol 105 (1) ◽  
pp. 279-288 ◽  
Author(s):  
M J Selwyn
Keyword(s):  
Adenosine Triphosphatase ◽  
Metal Cations ◽  
Coupling Factor ◽  
Heart Mitochondria ◽  
Aqueous Extracts ◽  
Bivalent Metal ◽  
Adenosine Triphosphatase Activity ◽  
General Properties ◽  
Kinetics Of

1. The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0° than at 25° but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg2+ or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg2+-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg2+ activation indicate that the ATP–Mg2+ complex is the important substrate: free ATP and Mg2+ are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).

An X-ray diffraction study of complexes of DNA and lactosyl-functionalised liposomes induced by bivalent metal cations: coexistence of different symmetries

2012 ◽  
Vol 40 (2) ◽  
pp. 137-148 ◽  
Author(s):  
Michela Pisani ◽  
Giovanna Mobbili ◽  
Milvia Marini ◽  
Oriano Francescangeli ◽  
Valerio Mori ◽  
...  
Keyword(s):  
Diffraction Study ◽  
Metal Cations ◽  
X Ray Diffraction ◽  
Bivalent Metal ◽  
X Ray

II. P-Tosyl Lysine and P-Tosyl Glutamic acid

1968 ◽  
Vol 23 (4) ◽  
pp. 429-430
Author(s):  
Joseph Reyes ◽  
Herschel Frye
Keyword(s):  
Aqueous Solution ◽  
Transition Metal ◽  
Glutamic Acid ◽  
Dissociation Constants ◽  
Metal Cations ◽  
Free Energies ◽  
Transition Metal Cations ◽  
Coordination Numbers ◽  
Dilute Aqueous Solution

Several complexes have been prepared with selected divalent transition metal cations and either p-tosyl lysine or p-tosyl glutamic acid; both acids were the L isomer. These complexes were synthesized in dilute aqueous solution and have been studied polarographically. Eight previously unreported compounds were prepared and studied, and their dissociation constants and coordination numbers are reported in this paper. The calculated Free Energies of Formation are also reported.

Molecular Models of the Stabilization of Bivalent Metal Cations in Zeolite Catalysts

2011 ◽  
pp. 579-643 ◽  
Author(s):  
G. M. Zhidomirov ◽  
A. A. Shubin ◽  
A. V. Larin ◽  
S. E. Malykhin ◽  
A. A. Rybakov
Keyword(s):  
Metal Cations ◽  
Zeolite Catalysts ◽  
Molecular Models ◽  
Bivalent Metal

Production and properties of α-amylase fromBacillussp. BKL20

2010 ◽  
Vol 56 (4) ◽  
pp. 279-288 ◽  
Author(s):  
Olha I. Kubrak ◽  
Janet M. Storey ◽  
Kenneth B. Storey ◽  
Volodymyr I. Lushchak
Keyword(s):  
High Activity ◽  
Yeast Extract ◽  
Culture Medium ◽  
Metal Cations ◽  
Culture Conditions ◽  
Bacillus Sp ◽  
Good Resistance ◽  
Bivalent Metal ◽  
Maximum Production ◽  
Ph Range

As a result of screening Bacillus sp. strains isolated from different natural substrates, strain BKL20 was identified as a producer of a thermostable alkaline α-amylase. Maximum production of this α-amylase was achieved by optimizing culture conditions. Production of α-amylase seemed to be independent of the presence of starch in the culture medium and was stimulated by the presence of peptone (0.3%, m/v) and yeast extract (0.2%, m/v). The enzyme was thermostable and retained amylolytic activity after 30 min of incubation at 60 and 70 °C. High activity was maintained over a broad pH range, from 6.0 to 11.0, and the enzyme remained active after alkaline incubation for 24 h. Bacillus sp. BKL20 α-amylase was not stimulated by Ca2+or other bivalent metal cations and was not inhibited by EGTA or EDTA at 1–10 mmol/L, suggesting that this α-amylase is a Ca2+-independent enzyme. It also showed good resistance to both oxidizing (H2O2) and denaturating (urea) agents.

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