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Quantitative Regeneration of Native Disulfide Bonds of Human Proinsulin

余宣传, 邹承鲁

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Abstract

It is well known that protein disulfide isomerase (PDI) catalyzes the thiol-disulfide exchange reactions and is believed to be responsible in the formation of disulfides during the synthesis of disulfide containing proteins. It has been reported in this laboratory that the native disulfide bonds of insulin can be regenerated from the scrambled or S-sulfonated chains with reasonably good yields and from the Al-B29 crosslinked insulin

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What this paper is about

It is well known that protein disulfide isomerase (PDI) catalyzes the thiol-disulfide exchange reactions and is believed to be responsible in the formation of disulfides during the synthesis of disulfide containing proteins. It has been reported in this laboratory that the native disulfide bonds of insulin can be regenerated from the scrambled or S-sulfonated chains with reasonably good yields and from the Al-B29 crosslinked insulin

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Available abstract

It is well known that protein disulfide isomerase (PDI) catalyzes the thiol-disulfide exchange reactions and is believed to be responsible in the formation of disulfides during the synthesis of disulfide containing proteins. It has been reported in this laboratory that the native disulfide bonds of insulin can be regenerated from the scrambled or S-sulfonated chains with reasonably good yields and from the Al-B29 crosslinked insulin

Key concepts: Protein disulfide-isomerase, Disulfide bond, Proinsulin, Chemistry, Thiol, Biochemistry, Insulin, Stereochemistry

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