Isolation And Characterization Of Collagen Type Ii From Poultry Trachea (Record no. 3046)

000 -LEADER
fixed length control field 03523nam a2200193Ia 4500
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20151005141019.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 150525s2011 xx 000 0 und d
041 ## - LANGUAGE CODE
Language code of text/sound track or separate title eng
082 ## - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 1330,T
100 ## - MAIN ENTRY--AUTHOR NAME
Personal name Sidra Ashraf
110 ## - MAIN ENTRY--CORPORATE NAME
Location of meeting Dr. Abu Saeed Hashmi
245 ## - TITLE STATEMENT
Title Isolation And Characterization Of Collagen Type Ii From Poultry Trachea
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Year of publication 2011
502 ## - DISSERTATION NOTE
Dissertation note This project was designed to use poultry waste to isolate and characterize collagen type II

from its trachea. Collagen type II is being used along with condroitin sulfate and

glucosamine for the treatment of osteoarthritis and is also available as a neutraceutical

product in the market. For project purpose, trachea of slaughtered broiler birds were

collected from the market and after removing adhering tissue and debris, it was then

washed thoroughly first with distilled water and then with deionized water. Tracheal

cartilage was then cut into small pieces and defattened with chloroform: methanol (2: 1

v/v) solution. After this, the cut pieces were properly cleaned with deionized water. 0.5%

Pepsin solution in 0.5 M acetic acid was prepared. Cartilage was then hydrolyzed by the

already prepared 0.5 % pepsin (in 0.5 M acetic acid) at 4 ° C for 48 hours. The extract
was then separated from the tracheal pieces and the viscous solution obtained was

centrifuged at 12000 rpm for 1 hr at 4 "c. Now the collagen was expected to be in the

supernatant which was salted out by adding NaCI to a final concentration of 2.5M and

kept for almost 12-16 hrs. This collagen was again centrifuged at 12000 rpm for 1 hr at

4 C. The obtained collagen pallet was redissolved in 0.5 M acetic acid and then it was

dialyzed against 0.1 M acetic acid followed by dialysis with distilled water. The sample

after dialysis was put in petri dishes and kept in freezer for overnight to let it be prepared for

lyophilization. The frozen collagen sample was then lyophilized. After lyophilization, the sample

gave an appearance of a white mesh. This sample was reconstituted in PBS with pH 8 to run it on

SDS-PAGE. The procedure of SDS-PAGE in non reducing conditions was adopted for the

characterization of collagen type II in the sample. The description of results of SDS-PAGE is given

below:

Lane M contains protein markers of different molecular weight. Lane 1, 2 and 3 contains

samples at different steps of the whole procedure showing clear bands of collagen type II.

Lane 4 contains lyophilized sample of collagen type II showing the thickest band (alpha

chain of collagen type II). In this research, poultry waste has been used for making health improving

product. As in our country poultry is used in bulk quantity so if its waste might be used in any

medicinal product then it might not only be useful but also economical for such a developing country

as ours. Another thing is that as this collagen Type II has been extracted from poultry trachea, it

shows that tracheal cartilage is a rich source of such collagen type. Collagen Type II is used in the

cure of arthritis especially rheumatoid arthritis so through this research, it has been made clear that

poultry waste can be utilized in a positive way in medicinal industry and also that collagen Type II

acts as an effective neutraceutical.
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical Term Institute of Biochemistry & Biotechnology
700 ## - ADDED ENTRY--PERSONAL NAME
Personal name Dr. Sualeha Riffat
700 ## - ADDED ENTRY--PERSONAL NAME
Personal name Zahid Mushtaq
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type Thesis
Holdings
Damaged status Collection code Permanent Location Current Location Shelving location Date acquired Full call number Accession Number Koha item type
  Veterinary Science UVAS Library UVAS Library Thesis Section 2015-05-29 1330,T 1330,T Thesis


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