Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Tumkur K"'
Autor:
Giri, Jyotsnendu, Sriharsha, Theerdhala, Asthana, Saket, Gundu Rao, Tumkur K., Nigam, Arun K., Bahadur, Dhirendra
Publikováno v:
In Journal of Magnetism and Magnetic Materials 2005 293(1):55-61
Publikováno v:
International Journal of Peptide and Protein Research. 13:153-160
Investigations have been carried out on the complex formed between sorghum Inhibitor III and alpha-chymotrypsin by physico-chemical methods. An apparent dissociation constant (Ki) of 4.0 X 10(-8) M has been calculated for the complex. This enzyme-inh
Autor:
Dhirendra Bahadur, A. K. Nigam, Theerdhala Sriharsha, Saket Asthana, Tumkur K. Gundu Rao, Jyotsnendu Giri
Publikováno v:
Journal of Magnetism and Magnetic Materials. 293:55-61
Substituted ferrites [Mn1−xZnxFe2O4 (0⩽x⩽0.8)] of nanoscale dimensions have been prepared by a novel microwave refluxing method. The effect of different parameters [such as pH, reflux time, presence of PEG (MW-3350) molecules] on particle morph
Autor:
Garg, Govind K.1, Virupaksha, Tumkur K.1
Publikováno v:
European Journal of Biochemistry. 1970, Vol. 17 Issue 1, p13-18. 6p.
Publikováno v:
Biochemical Systematics and Ecology. 21:499-504
Lectin pattern of Vigna glabrescens, a naturally occurring allotetraploid, was studied as a guide to determine its probable parents. Lectin patterns of a few of the synthetic allotetraploids and their known parents were also studied for purposes of c
Publikováno v:
Journal of the Science of Food and Agriculture. 54:367-378
Nine varieties of finger millet (Eleusine coracana Gaertn) including a wild form were screened for proteinase and α-amylase inhibitory activities. Subtilisin inhibitory activity was present in all the varieties examined and was highest in the wild f
Publikováno v:
Journal of Food Biochemistry. 14:45-59
Germinating seeds of Cassia sericea Sw. contain two molecular forms of α-galactosidase which were partially purified and characterized. Both enzyme forms had an optimum pH of 5.0 and an optimum temperature of 50 °C. Km values for the substrate p-ni
Publikováno v:
Phytochemistry. 29:1763-1766
A crystalline protease, artocarpin, isolated from Artocarpus heterophyllus fruit latex, consisted of a single polypeptide of Mr 79 500. The pH optimum was 8.0 and pI 6.3. It was activated by thiol reducing reagents, and inhibited by phenylmethylsulph
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Akademický článek
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