Some structural characteristics of linamarase from cassava (Manihot esculenta Crantz.)
Issued Date
2024
Copyright Date
1989
Resource Type
Language
eng
File Type
application/pdf
No. of Pages/File Size
xii, 94 leaves : ill.
Access Rights
open access
Rights
ผลงานนี้เป็นลิขสิทธิ์ของมหาวิทยาลัยมหิดล ขอสงวนไว้สำหรับเพื่อการศึกษาเท่านั้น ต้องอ้างอิงแหล่งที่มา ห้ามดัดแปลงเนื้อหา และห้ามนำไปใช้เพื่อการค้า
Rights Holder(s)
Mahidol University
Bibliographic Citation
Thesis (M.Sc. (Biochemistry))--Mahidol University, 1989
Suggested Citation
Pennapa Kisamanonta Some structural characteristics of linamarase from cassava (Manihot esculenta Crantz.). Thesis (M.Sc. (Biochemistry))--Mahidol University, 1989. Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/100178
Title
Some structural characteristics of linamarase from cassava (Manihot esculenta Crantz.)
Alternative Title(s)
คุณสมบัติทางโครงสร้างบางรประการของเอนาไซม์ลินามาเรสจากมันสำปะหลัง
Author(s)
Abstract
Three isozyme of cassava petiole linamarase were used in two types of studies : structural study and subunit interaction study. Native isozymes were insensitive to the following protease: trypsin pronase, thermolysin, papain, subtilisin, collagenase and bromelain. After denaturation, they became sensitive to trypsin, pronase and thermolysin and yielded similar proteolytic fragments suggesting a simlar protein chain among the isozymes. using TNBS to modify lysine residues, the native and denatured forms of the isozyme pI 4.3 were found to have 179 and 199 mole lysines/mole isozyme respectively. Similarly, the native and denatured forms the isozyme pI 2.9 contained 88 and 100 moles/mole respectively. In the presence of a competitive inhibitor, the number of modified lysines of the native isozymes were not changed. The data indicated that most lytic site. The isozymes were probably glycoproteins since they can be retained by a Con A-Sepharose column. The anti-linamarase serum was able to recognize the modified isozymes except isozyme pI 2.9 but could not recognize the heat-denatured isozymes. Guanidine hydrochloride dissociated the enzyme into smaller forms and caused inactivation also. Complete inactivation was observed by 3M GuHC1. However, the isozymes were stable in SDS up to 20% at room temperature for 30 min. In SDS-PAGE containing 1% SDS, active forms of different sizes were found. Treatment with β-mercaptosthanol did not dissociate the enzyme into subunits but heat treatment caused the dissociation and the complete loss of the activity.
Description
Biochemistry (Mahidol University 1989)
Degree Name
Master of Science
Degree Level
Master's degree
Degree Department
Faculty of Science
Degree Discipline
Biochemistry
Degree Grantor(s)
Mahidol University