2 edition of purification and study of cathepsin D from bovine spleen. found in the catalog.
purification and study of cathepsin D from bovine spleen.
Anne Mary Freeman
PhD thesis, Biochemistry.
The enzyme was purified from liver of man and chicken by a procedure involving autolysis, acetone fractionation, ion-exchange chromatography and isoelectric focusing. 3. Several isoenzymes of cathepsin D were resolved in the isoelectric-focusing step, and three major forms, α,β and γ, were distinguished for each by: The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleenCited by:
Application. Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels. 6. Human cathepsin D had a pH optimum of , and that of chicken enzyme was , haemoglobin being used as substrate. In each species, the three isoenzymes have the same pH-dependence curve. 7. The purified cathepsin D samples showed very Cited by:
on the selectivity of cathepsin D under correspondingly mild conditions (e.g. 16). In this paper we report on a study of the selectivity bovine spleen cathepsin D during limited proteolysis of var- ious substrates of known primary structure. Proteins used in this study are sperm whale myoglobin, hen egg-white lyso-. Cathepsin B, Bovine Spleen One of the most investigated lysosomal cysteine proteinases that is widely Cathepsin Inhibitor II 10 U distributed in a variety of tissues. Cathepsin D, Bovine Kidney A major lysosomal aspartic proteinase widely distributed in many cell Size: KB.
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This chapter focuses on the purification, characterization, and structural studies of bovine spleen cathepsins D and S. It is known that lysosomal proteases play an important role in the normal turnover of tissue by: 5.
The purification and study of Cathepsin D from bovine spleen Author: Freeman, A. ISNI: Awarding Body: University of Salford Current Institution: University of Salford Date of Award: Availability of Full Text: Access from EThOS.
The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C, gel filtration on Sephacryl S and chromatofocusing (pH ). The enzyme was partially destroyed by autolysis of the homogenate at pH The isoelectric point of cathepsin S was Cited by: The purification and study of Cathepsin D from bovine spleen.
(Thesis) Freeman AM. Publisher: University of Salford  Metadata Source: The British Library Type: Thesis. Abstract. No abstract supplied. Menu. Formats. Abstract. EThOS. About. About Europe PMC; Funders; Joining Europe PMC; Governance Author: Freeman Am.
available source of tissue for further enzyme purification at- tempts. As purification of the hemoglobin-digesting activity at pH progressed, it became obvious that the responsible enzyme was a form of cathepsin D similar to that described in bovine spleen by Press, Porter, and Cebra (3).
Although the purification of cathepsin D has been reported from a number of sources, including bovine spleen and other bovine tissues (l-7), chicken liver (8), porcine thyroid (9, lo), porcine intestinal mucosa (ll), and human red blood cells (la), the enzyme has not been obtained in large quantity.
Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimer’s disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic human foreskin fibroblasts.
Cathepsin D-Bovine Cat D-Bovine - - NaH 2 PO 4 +H 2 O Sodium phosphate, monobasic, monohydrate/ Monosodium phosphate - Concentration ≥52% ≤48% 4. FIRST AID MEASURES Inhalation If inhaled, move person into fresh air. If not breathing, give CPR. Pseudorenin and cathepsin D activity from bovine spleen were found to behave identically on DEAE-cellulose, Sephadex G, and concanavalin A-agarose Cited by: 5.
The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C, gel filtration on Sephacryl S. Following the pub- lication by Press et al. () on the purification of cathepsin D from bovine spleen, numerous reports on the purification of similar activities in Correspondence to: S.
Rimon, Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Cited by: Press E. M., Porter R. and Cebra J.
() The isolation Purification of insect cathepsin D 83 and properties of a proteolytic enzyme, cathepsin D, from bovine spleen. Biochem. 74, Cited by: 4. action of cathepsin D from the standpoint developed in the case of pepsin (22, 24). In connection with this work, a method for the purification of cathepsin D from bovine spleen was devised; since this procedure differs significantly from those described by other investigators, the details are reported here.
had been observed in cathepsin D preparations from bovine spleen (8). However, many workers have described prepara- tions of cathepsin D without noting multiple forms. This raised the important question of whether these multiple forms exist in nature or whether they are artifacts caused by certain.
study of cathepsin D from rat spleen because cathep- sin D from rat spleen has not been extensively studied and a specific activity of the enzyme in this organ is about 5 times higher than that of the liver. Recently Enzyyme. Cathepsin D (EC ). several workers have isolated cathepsin D by affinityCited by: 1.
Methods Enzymol. ;80 Pt C Cathepsin D from porcine and bovine spleen. Takahashi T, Tang J. PMID: [PubMed - indexed for MEDLINE]Cited by: The purification and study of Cathepsin D from bovine spleen. By A Freeman. Abstract. SIGLEAvailable from British Library Document Supply Centre- DSC:D/84 / BLDSC - British Library Document Supply CentreGBUnited Kingdo Topics: 06A - Biochemistry Author: A Freeman.
The V m /K m. app value for bovine cathepsin D was higher than that for ostrich cathepsin D ( and ∆A nm /45 min/mg enzyme/μM, respectively), which is in good agreement with that obtained for bovine spleen cathepsin D (∆A nm /60 min/mg enzyme/μM) by Ferguson, Andrews, Voynick, and Fruton (). This implies that bovine Cited by: 9.
The purified enzyme was the major isoenzyme, which represented 60% of cathepsin D present in porcine spleen. Two minor isoenzymes of cathepsin D were present in small amounts.
cathepsin D. Purification, crystallization and preliminary X- Studies of bovine spleen cathepsin D. Acta Biol Med. ; A literature survey was performed of human cathepsin D.
Multiple forms of Cathepsin D from bovine uterus. May ; study that the enzyme may consist of a single polypeptide chain. of the spleen enzyme and the human and chicken liver enzyme.
2. The first step of the purification consists in suspending frozen and thawed spleen in water and letting it autolyze. 3. In the second step, ammonium sulfate is added and the suspension is acidified and warmed. Much additional autolysis takes place. The cathepsin is protected from destruction by being adsorbed to the insoluble spleen material.SPBovine- Cathepsin B, Bovine Spleen Athens Research & Technology Athens Research and Technology, Inc.
SDS - SAFETY DATA SHEET 1. IDENTIFICATION PRODUCT NAME Cathepsin B, Bovine Spleen PRODUCT NO. SPBovine BRAND Athens Research and Technology Use of substance Research Reagent SUPPLIER Athens Research and Technology.