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A study of enzyme proteolysis: A un...

Powell, Stavroula Panagiotopoulos.

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A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme./
Author:	Powell, Stavroula Panagiotopoulos.
Description:	79 p.
Notes:	Source: Masters Abstracts International, Volume: 43-05, page: 1729.
Contained By:	Masters Abstracts International43-05.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1425523
ISBN:	0496987526

A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme.
Powell, Stavroula Panagiotopoulos.

A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme. - 79 p.

Source: Masters Abstracts International, Volume: 43-05, page: 1729.

Thesis (M.S.)--University of Massachusetts Lowell, 2005.

One of the major proteins found in tears is lysozyme. Lysozyme has been long studied for its enzymatic capabilities. As an enzyme, it catalyzes the cleavage of glycosidic bonds. As a protein, lysozyme is very basic. This is due to the presence of many lysine and arginine amino acids. Studies have shown that fragments of protein, versus the intact protein, tend to cling to contact lenses. When lysozyme is digested by subtilisin, fragments that result tend to be of similar molecular size. Studies have also shown that disulfide bonds help stabilize the protein deposits on contact lenses. The lysozyme molecule contains four disulfide bridges.

ISBN: 0496987526Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme.
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008 130610s2005 eng d
020 $a 0496987526
035 $a (UnM)AAI1425523
035 $a AAI1425523
040 $a UnM $c UnM
100 1 $a Powell, Stavroula Panagiotopoulos. $3 1903521
245 1 2 $a A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme.
300 $a 79 p.
500 $a Source: Masters Abstracts International, Volume: 43-05, page: 1729.
500 $a Supervisor: Edwin G. E. Jahngen.
502 $a Thesis (M.S.)--University of Massachusetts Lowell, 2005.
520 $a One of the major proteins found in tears is lysozyme. Lysozyme has been long studied for its enzymatic capabilities. As an enzyme, it catalyzes the cleavage of glycosidic bonds. As a protein, lysozyme is very basic. This is due to the presence of many lysine and arginine amino acids. Studies have shown that fragments of protein, versus the intact protein, tend to cling to contact lenses. When lysozyme is digested by subtilisin, fragments that result tend to be of similar molecular size. Studies have also shown that disulfide bonds help stabilize the protein deposits on contact lenses. The lysozyme molecule contains four disulfide bridges.
520 $a In the contact lens industry, the standard method of cleaning efficacy for contact lenses using proteases, is N,N-dimethyl casein (DMC). The proteolytic enzyme method using DMC monitors free amines; thus it monitors the rate of amine formation. Since protease breakdown lysozyme, it seems to be a more appropriate technique to use lysozyme in looking at proteolysis in tears or enzyme cleaners, rather than casein.
590 $a School code: 0111.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0487
690 $a 0486
710 2 0 $a University of Massachusetts Lowell. $3 1017839
773 0 $t Masters Abstracts International $g 43-05.
790 1 0 $a Jahngen, Edwin G. E., $e advisor
790 $a 0111
791 $a M.S.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1425523