Malate synthase activity in cotton and other ungerminated oilseeds: a survey.

نویسندگان

  • J A Miernyk
  • R N Trelease
  • J S Choinski
چکیده

Extracts from several species and varieties of ungerminated cotton seeds plus homogenates from 18 other oilseeds (representing 11 different families) were examined for malate synthase and isocitrate lyase activity. Malate synthase activities in the various cotton seeds ranged from 35 to 129% of the units per dry seed weight found in Deltapine 16 cotton. For other oilseeds, the range was from 0.3 to 58% of Deltapine 16 cotton. Castor bean (Ricinus communis L.) had the least activity per mg dry weight (12-fold lower than the next lowest species), while Pima cotton (Gossypium barbadense L.) had the highest level (8.53 units). On a per seed basis, these values were 15 and 747 nanomoles per minute.Malate synthase activity was measurable in all seed types examined, whereas isocitrate lyase could not be detected in any of the seeds. We suggest that synthesis of malate synthase during seed development is universal among oilseeds in the absence of glyoxylate-cycle-associated isocitrate lyase activity.

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

Cottonseed malate synthase : purification and immunochemical characterization.

Malate synthase (EC 4.1.3.2), an enzyme unique to the glyoxylate cycle, was purified to homogeneity from cotyledons of 72-hours, darkgrown cotton (Gossypium hirsutum L.) seedlings. Homogeneity of the enzyme was assessed by silver staining SDS-PAGE gels. Purification was accomplished by using a single buffer medium through six steps involving one ammonium sulfate fractionation and chromatography...

متن کامل

Role of malate synthase in citric Acid synthesis by maturing cotton embryos: a proposal.

Cotton embryos from 34 to 54 days after anthesis were analyzed for organic acids, and enzymes associated with organic acid metabolism. During this developmental period, embryos accumulated citrate. Malate synthase activity appeared at 46 days after anthesis and increased rapidly to 54 days. Of other enzymes examined, only citrate synthase activity increased during this period. As isocitrate lya...

متن کامل

Nucleotide sequence of cottonseed malate synthase.

We report the nucleotide sequence of a cDNA clone encoding S-K-L has been reported to be a peroxisomal trafficking signal the complete amino acid sequence of the glyoxysomal enzyme in mammals (6). malate synthase (MS) (EC 4.1.3.2) in cotton seeds. A cDNA library was constructed in UNI-ZAP (Stratagene) from ACKNOWLEDGEMENT poly(A) + RNA extracted from cotyledons of 48-h-grown seedlings and scree...

متن کامل

Photosynthetic Characteristics and Antioxidative Responses in Three Species of Crassulaceae Following Drought Stress

Photosynthetic characteristics and induction of crassulacean acid metabolism (CAM) by drought stress were investigated in Sedum album, Sedum stoloniferum and Rosularia elymaitica from Crassulaceae. Titratable acidity, malate content, phosphoenolpyruvate carboxylase (PEPC) activity and gas exchange parameters were determined in plants at the end and beginning of the photoperiod. Results showed t...

متن کامل

Differential Contribution of Malic Enzymes during Soybean and Castor Seeds Maturation

Malic enzymes (ME) catalyze the decarboxylation of malate generating pyruvate, CO2 and NADH or NADPH. In some organisms it has been established that ME is involved in lipids biosynthesis supplying carbon skeletons and reducing power. In this work we studied the MEs of soybean and castor, metabolically different oilseeds. The comparison of enzymatic activities, transcript profiles and organic ac...

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:
  • Plant physiology

دوره 63 6  شماره 

صفحات  -

تاریخ انتشار 1979