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Coefficient Estimate of bi-Bazilevič Functions Associated with Fractional q-calculus Operators

Murugusundaramoorthy G., Janani T., Purohit S. D.

Fundamenta Informaticae

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2017

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Vol. 151, nr 1/4

49--62

EN

In this paper, we introduce and investigate two new subclasses of the function class ∑ of bi-univalent functions defined in the open unit disk, which are associated with fractional q-calculus operators, satisfying subordinate conditions. Furthermore, we find estimates on the Taylor-Maclaurin coefficients |a2| and |a3| for functions in these new subclasses. Several (known or new) consequences of the results are also pointed out.

2

Majorization problems for classes of analytic functions

Dziok J., Murugusundaramoorthy G., Janani T

Journal of Mathematics and Applications

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2015

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Vol. 38

49--57

EN

The main object of the present paper is to investigate problems of majorization for certain classes of analytic functions of complex order defined by an operator related to the modified Bessel functions of first kind. These results are obtained by investigating appropriate class of admissible functions. Various known or new special cases of our results are.

3

Binding of harmane to human and bovine serum albumin: fluorescence and phosphorescence study

Gałęcki K, Despotović B, Ioannidis A.-G, Janani T, Galloway C, Nakamura Y, Oluyinka G

Biotechnology and Food Science

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2012

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Vol. 76, nr 1

3--12

EN

The binding of harmane with human serum albumin (HSA) and bovine serum albumin (BSA) were studied by fluorescence and phosphorescence spectroscopic methods. Quenching of fluorescence of serum albumins by harmane was found to be a static quenching process. The equilibrium constant (K) of complex formation was found to be equal to (5.16±0.28)x104 M-1 and (4.32±0.30)x104 M-1 for HSA and BSA, respectively. It was found that the interactions of harmane with HSA and BSA were also in the excited triplet state. The determined bimolecular constant or triplet state quenching (kqT)of the proteins studied by harmane was (1.15± 0.10)x107 M-1 s-1 and (2.88±0.22)x107 M-1 s-1 for HSA and BSA, respectively. Based on the similar value of K and kqT for HSA and BSA, a possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa.