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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.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme./
作者:	Powell, Stavroula Panagiotopoulos.
面頁冊數:	79 p.
附註:	Source: Masters Abstracts International, Volume: 43-05, page: 1729.
Contained By:	Masters Abstracts International43-05.
標題:	Chemistry, Biochemistry. -
電子資源:	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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245 1 2 $a A study of enzyme proteolysis: A unique look at the hydrolysis of lysozyme.
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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.
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