Deciphering proteolytic processing of carbonic anhydrase 1 from Chlamydomonas reinhardtii

نویسندگان

  • Parijat S. Juvale
  • Martin H. Spalding
  • Diane C. Bassham
  • Drena L. Dobbs
چکیده

iii GENERAL INTRODUCTION 1 PART 1. DECIPHERING PROTEOLYTIC PROCESSING OF PERIPLASMIC CARBONIC ANHYDRASE 1(CAH1) 9

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Identification of Intracellular Carbonic Anhydrase in Chlamydomonas reinhardtii which Is Distinct from the Periplasmic Form of the Enzyme.

A physiologically significant level of intracellular carbonic anhydrase has been identified in Chlamydomonas reinhardtii after lysis of the cell wall-less mutant, cw15, and two intracellular polypeptides have been identified which bind to anti-carbonic anhydrase antisera. The susceptibility of the intracellular activity to sulfonamide carbonic anhydrase inhibitors is more than three orders-of-m...

متن کامل

Partial characterization of a new isoenzyme of carbonic anhydrase isolated from Chlamydomonas reinhardtii.

A new isoenzyme of carbonic anhydrase has been isolated and purified from Chlamydomonas reinhardtii. This carbonic anhydrase is composed of two nonidentical subunits with apparent molecular masses of 39 and 4.5 kDa and is located in the periplasmic space. This is the second periplasmic carbonic anhydrase found in C. reinhardtii. Two genes, CAH1 and CAH2, which code for carbonic anhydrase, have ...

متن کامل

Identification of Intracellular Carbonic Anhydrase in Chiamydomonas reinhardtii which Is Distinct from the Periplasmic Form of the Enzyme 1

A physiologically significant level of intracellular carbonic anhydrase has been idenfified in Chlamydomonas reinhardtii after lysis of the cell wall-less mutant, cw15, and two intracellular polypeptides have been identified which bind to anti-carbonic anhydrase antisera. The susceptibility of the intracellular activity to sulfonamide carbonic anhydrase inhibitors is more than three orders-of-m...

متن کامل

Identification of Extracellular Carbonic Anhydrase of Chlamydomonas reinhardtii.

We have examined the induction of carbonic anhydrase activity in Chlamydomonas reinhardtii and have identified the polypeptide responsible for this activity. This polypeptide was not synthesized when the alga was grown photoautotrophically on 5% CO(2), but its synthesis was induced under low concentrations of CO(2) (air levels of CO(2)). In CW-15, a mutant of C. reinhardtii which lacks a cell w...

متن کامل

bicarbonate-carbon dioxide exchange catalyzed by extracellular carbonic anhydrase in Chlamydomonas reinhardtii

Acetate assimilation in C. reinhardtii leads to bicarbonate and CO2 aq formation in heterotrophic growth condition. Bicarbonate and CO2 aq thus formed under this condition remain in equilibrium with the action of carbonic anhydrases. Carbonic anhydrase catalyzes reversible hydration of carbon dioxide and dehydration of bicarbonate. In this article we report that the rapid exchange catalyzed by ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2017