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D. Mayilvahanan G. Annadurai V. Raju M. Chellapandian M. R. V. Krishnan Kunthala Jayaraman 《Bioprocess and biosystems engineering》1996,15(6):323-326
Techniques for possible higher and rapid production of citric acid from the well known industrial medium i.e. molasses has
been reported using Aspergillus niger. This includes optimization of the total reducing sugar (TRS) and nutrients like nitrogen
and phosphorous. The long and unproductive lag periods normally associated with this type of fermentation has been reduced.
These strategies are discussed in detail.
Dr. M. Chellapandian is thankful to the Council of Scientific and Industrial Research, New Delhi, for the award of research
associateship. 相似文献
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FK506 binding protein associated with the calcium release channel (ryanodine receptor). 总被引:31,自引:0,他引:31
T Jayaraman A M Brillantes A P Timerman S Fleischer H Erdjument-Bromage P Tempst A R Marks 《The Journal of biological chemistry》1992,267(14):9474-9477
The calcium release channel (CRC)/ryanodine receptor (RyRec) has been identified as the foot structure of the sarcoplasmic reticulum (SR) and provides the pathway for calcium efflux required for excitation-contraction coupling in skeletal muscle. The CRC has previously been reported to consist of four identical 565-kDa protomers. We now report the identification of a 12-kDa protein which is tightly associated with highly purified RyRec from rabbit skeletal muscle SR. N-terminal amino acid sequencing and cDNA cloning demonstrates that the 12-kDa protein from fast twitch skeletal muscle is the binding protein for the immunosuppressant drug FK506. In humans, FK506 binds to the 12-kDa FK506-binding protein (FKBP12) and blocks calcium-dependent T cell activation. We find that FKBP12 and the RyRec are tightly associated in skeletal muscle SR on the basis of: 1) co-purification through sequential heparin-agarose, hydroxylapatite, and size exclusion chromatography columns; 2) coimmunoprecipitation of the RyRec and FKBP12 with anti-FKBP12 antibodies; and 3) subcellular localization of both proteins to the terminal cisternae of the SR, and not in the longitudinal tubules of SR, in fast twitch skeletal muscle. The molar ratio of FKBP12 to RyRec in highly purified RyRec preparations is approximately 1:4, indicating that one FKBP12 molecule is associated with each calcium release channel/foot structure. 相似文献
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Summary A simple and rapid detection of proteolytic activity of microbial sources on a thermally reversible gel (Pluronic F-127) is described. 相似文献
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AbstractPhenolic compounds such as catechol and resorcinol are toxic and persistent pollutants in the aqueous environment. Detection procedures such as chromatographic and spectrophotometric methods are time-consuming and require sophisticated instruments with skilled manpower. Development of a simple, cost effective, portable and disposable paper based biosensor could be a better alternative to the conventional methods. The present study attempted to develop a paper based biosensor by immobilizing horseradish peroxidase enzyme to detect catechol and resorcinol in aqueous samples. Horseradish peroxidase catalyzes the oxidation of phenolic compounds to semiquinones, which on reaction with a chromogen, 3-methyl 2-benzothiazolinone hydrazine (MBTH) gives faint pink to red color depending on the compound and its concentration in the sample is the basis for biosensing application. Different methods of enzyme immobilization on filter paper like physical adsorption, covalent coupling, and polysaccharide entrapment were executed. The performance of the various enzyme immobilization methods was evaluated by analyzing the developed color intensity using ImageJ software. Entrapment technique is the most effective method of immobilizing enzyme on the filter paper that produces the highest color intensity with better stability. The visible limit of detection (LoD) was observed as 0.45?mM (50?mg/L) for catechol and 0.09?mM (10?mg/L) for resorcinol in aqueous samples. 相似文献