Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 208 (1987), S. 271-278 
    ISSN: 1617-4623
    Keywords: ADH ; Enzyme activation ; Isozyme ; Antibody ; Maize
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Antisera were raised against several purified, high specific acitivity isozymes of maize alcohol dehydrogenase (ADH1). The various antisera had different effects on the activity of immunoprecipitated ADH. One antiserum completely inactivated maize ADH. This inactivation could be blocked by preicubation of the enzyme with NAD+, its cofactor, or with NADP. The different antisera were used to analyze variant froms of ADH1. Isozymes having lowered specific activity were activated to wild-type levels by precipitation of the enzymes with noninactivating antisera. Isozymes having no detectable ADH activity (CRM+ nulls) were activated by immunoprecipition with noninactivating antisera when preincubated with NAD+ or NADP. All of the CRM+ nulls were shown to be unable to bind NAD+, a flaw which can account for their lack of activity. The results indicate that a conformational equilibrium between active and inactive forms of maize ADH in solution controls the specific activity of the various isozymes. Both controls the specific activity of the various isozymes. Both NAD+ and antibodies raised against high specific activity enzymes can interact with low activity isozymes to shift the balance of the equilibrium toward the active form, thus increasing their specific activity.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...