1991
DOI: 10.1007/bf01025627
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Protection and enhancement of ribulose 1,5 bisphosphate carboxylase activity by exogenous proteins

Abstract: When assayed in vitro, the activity of the photosynthetic enzyme ribulose 1,5 bisphosphate carboxylase oxygenase is both enhanced and protected from spontaneous decay by exogenous proteins such as hemoglobin, serum albumin, and aldolase. Other proteins and amino acids tested are either ineffective (lysozyme, ferritin, lysine, and cysteine) or afford only partial protection (catalase, glycine, and phenylalanine). Protective proteins do not bind to, or exchange disulfides with, ribulose 1.5 bisphosphate carboxyl… Show more

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“…1, black bars). This result suggests a higher sensitivity of RUBISCO from diatoms to oxidation (which might result from mild oxidizing conditions along the purification process), when compared to RUBISCO from C. reinhardtii and other green‐like RUBISCOs (Peñarrubia and Moreno 1991, Garcia‐Ferris and Moreno 1993).…”
mentioning
confidence: 97%
“…1, black bars). This result suggests a higher sensitivity of RUBISCO from diatoms to oxidation (which might result from mild oxidizing conditions along the purification process), when compared to RUBISCO from C. reinhardtii and other green‐like RUBISCOs (Peñarrubia and Moreno 1991, Garcia‐Ferris and Moreno 1993).…”
mentioning
confidence: 97%