東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Purification and characterization of...

Weerasinghe, Vasana Chandani.

Linked to FindBook

Google Book

Amazon

博客來

Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss).

Record Type:	Electronic resources : Monograph/item
Title/Author:	Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss)./
Author:	Weerasinghe, Vasana Chandani.
Description:	289 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1018.
Contained By:	Dissertation Abstracts International64-03B.
Subject:	Agriculture, Food Science and Technology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3082574
ISBN:	0496304259

Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss).
Weerasinghe, Vasana Chandani.

Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss). - 289 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1018.

Thesis (Ph.D.)--University of California, Davis, 2003.

The use of proteolytic enzymes from marine organisms as processing aids is becoming more widespread due to their unique properties, and their unique habitat conditions, compared to enzymes from mammalian sources. Furthermore, different fish species exhibit different properties depending on their environment, making them potential sources of enzymes for different applications. Fish guts are a good and cheap source of proteolytic enzymes, and they are produced in mass quantities, as a byproduct, during the processing of fish.

ISBN: 0496304259Subjects--Topical Terms:

1017813
Agriculture, Food Science and Technology.

Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss).
LDR:03413nmm 2200337 4500 001 1845582
005 20051101072033.5
008 130614s2003 eng d
020 $a 0496304259
035 $a (UnM)AAI3082574
035 $a AAI3082574
040 $a UnM $c UnM
100 1 $a Weerasinghe, Vasana Chandani. $3 1933738
245 1 0 $a Purification and characterization of gastric proteases from rainbow trout (Oncorhynchus mykiss).
300 $a 289 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1018.
500 $a Adviser: N. F. Haard.
502 $a Thesis (Ph.D.)--University of California, Davis, 2003.
520 $a The use of proteolytic enzymes from marine organisms as processing aids is becoming more widespread due to their unique properties, and their unique habitat conditions, compared to enzymes from mammalian sources. Furthermore, different fish species exhibit different properties depending on their environment, making them potential sources of enzymes for different applications. Fish guts are a good and cheap source of proteolytic enzymes, and they are produced in mass quantities, as a byproduct, during the processing of fish.
520 $a The gastric juice of vertebrates contains aspartic proteinases, which are secreted as zymogens and undergo conversion to active enzymes in the acidic conditions of the gastric environment. The major gastric proteases are pepsin, gastricsin, and chymosin. The classification of gastric proteases from aquatic organisms is not very well understood. Zymogens of proteases were extracted from stomachs, purified, and characterized in order to assess whether they are pepsin-like, gastricsin-like, chymosin-like or cathepsin D-like.
520 $a The pepsin activity of 6 month old rainbow trout increased with increasing water salinity, while no influence was seen on 12 month old rainbow trout and steelhead trout. Pepsin activity was highest in the steelhead trout at all the salinities, compared to that of rainbow trout.
520 $a Five zymogens (I--V) for gastric proteases were isolated. The order of elution from the DEAE cellulose column was I, II, IV, V, and III. From activity staining, III is the major zymogen, followed by II, I, V, and IV. Zymogen I was not retained by DEAE cellulose under the experimental conditions, and its activity was negligible unless the assay solutions contained NaCl. Activity staining in the presence of pepstatin and in the hemoglobin assay showed that zymogens V and IV were less sensitive to pepstatin than were the other isoforms and mammalian pepsin. Synthetic substrate APDT was scarcely hydrolyzed by any of the zymogens.
520 $a The structural characteristics such as molecular weight by SDS-PAGE, amino acid analysis, N-terminal sequence, and peptide mass mapping and some internal sequencing were performed on all the separated zymogens and activated enzymes. The structural homology of trout gastric zymogens with pepsin, gastricsin and chymosin was evaluated. Zymogens I, II and III appeared to be more pepsin-like, while zymogens V and IV appeared to be more gastricsin-like.
590 $a School code: 0029.
650 4 $a Agriculture, Food Science and Technology. $3 1017813
650 4 $a Agriculture, Fisheries and Aquaculture. $3 1020913
650 4 $a Biology, Molecular. $3 1017719
690 $a 0359
690 $a 0792
690 $a 0307
710 2 0 $a University of California, Davis. $3 1018682
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Haard, N. F., $e advisor
790 $a 0029
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3082574