John’s Baptism and Christian Baptism: A Comparative Study (original) (raw)

Progressive Study on the Physiological Role and Catalytic Properties of Buffalo Lung Cathepsin B

https://www.ijhsr.org/IJHSR\_Vol.8\_Issue.10\_Oct2018/IJHSR\_Abstract.08.html, 2018

Physiological and catalytic properties of cathepsin B from water buffalo (Bubalus bubalis) lung, hitherto unstudied source/tissue, have been reported. The activity of the enzyme was optimal at physiological temperature (37°C) and the enzyme could withstand temperature shocks up to 37°C for 10-30 min without any significant loss of activity. Moreover the maximum activity was observed at pH 7.0 and the enzyme was fairly stable between pHs 3.5-6.75 for at least 20 min. Cathepsin B was most active at 2.5x10-3 M buffer concentration and lost its activity substantially as the buffer concentration was raised above optimum value. As the enzyme was highly stable between salt concentrations of 1.5x10-2 M to 3.5x10-2 M, it is recommended to store the enzyme in 0.05 M sodium phosphate or other buffer of equivalent ionic strength. The buffalo lung enzyme hydrolyzed Z-Phe-Arg-MCA (V max /K m =13.21) was found to be the most efficient substrate followed by Z-Arg-Arg-MCA, BANA and BAPNA. The preferred protein substrate for the enzyme is found to be haemoglobin. The enzyme also hydrolyzed other protein substrates such as bovine serum albumin, ovalbumin and casein, but to lesser extents. In contrast to prevailing opinion, it was concluded that cathepsin B can act for a limited period even at physiological temperature, pH and salt concentration before it is inactivated.

On the tissue/species dependence of cathepsin B isozymes

Molecular and cellular biochemistry, 1997

Characterization of cathepsin B from buffalo kidney and goat spleen showed the presence of isozymes in case of the goat spleen (GSCB-I and GSCB-II) whereas cathepsin B from buffalo kidney exhibited only one form (BKCB). The molecular weights determined by SDS-PAGE for GSCB-I, GSCB-II, and BKCB were 25.7, 26.6 and 25.5 kDa respectively. The kinetic parameters (Km and Vmax) of GSCB-I showed close similarities with BKCB against alpha-N-benzoyl-DL-arginine-2-napthylamide whereas GSCB-II was closer to the buffalo enzyme with regards to its activity against Z-Arg-Arg-MCA and Z-Phe-Arg-MCA. All the three enzymes had similar sensitivities towards urea, antipain and leupeptin. However, clear differences were observed in the inhibition patterns of the enzyme with iodoacetic acid and iodoacetamide. Differences in the kinetic, immunogenic and some catalytic properties of GSCB-I and II, which had similarities with regard to most of their physico-chemical properties, were considered to be due to ...

Cathepsins D from rhesus monkey lung. Purification and characterization

Journal of biochemistry, 1980

Two types of cathepsin D (cathepsins D-I and D-II) were purified from rhesus monkey lung to homogeneity as judged from disc gel electrophoresis. Cathepsin D-I was purified about 2,000-fold with a 5.1% yield while cathepsin D-II was purified about 2,300-fold with a 14.3% yield. Both cathepsins D were rich in the lysosome fraction of the lung, but appeared to be present in part extracellularly. Both showed a molecular weight of about 35,000 on Sephadex G-100 chromatography, and about 41,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cathepsin D-I showed the maximal activity on bovine hemoglobin and albumin at pH 3.4 and 4.0, respectively. It was most stable in the pH range of 5 to 7, but was rather unstable outside this pH range. Cathepsin D-II was quite similar in properties to that from Japanese monkey lung (Moriyama, A. & Takahashi, K. (1978) J. Biochem. 83, 441-451), and was remarkably stable in the pH range of 1-9. Under the conditions used, it retained at leas...