The Four Types Of Thiioredoxins In Plants

Hobart and William Smith Colleges. (2017). Lab 04 BIOL 1510 Lab Manual Plant Defenses F2017 - Biology - StuDocu. Retrieved from https://www.studocu.com/en/document/hobart-and-william-smith-colleges/biology/lecture-notes/lab-04-biol-1510-lab-manual-plant-defenses-f2017/1396233/view

vulgaris plants, via the formation of a standard curve prepared using varying concentrations of bovine serum albumin (BSA) solution. Following absorbance readings of the various BSA solutions, they were plotted against their concentrations providing an indirect measure for determining protein concentrations of the plant samples within the assay tubes, and through further calculations the sample protein concentration. The mean protein concentration for the control group was calculated to be 3.34 ± 1.30 mg/mL, while the mean treated group concentration was 2.01 ± 1.26 mg/mL. These results similarly like the chlorophyll results correlate with the literature articles, as a reduced protein content within the Paraquat treated plants can be expected to some extent (Chia et al., 1981). This reduction in protein concentration is the result of those superoxide anions produced by Paraquat, disrupting the chloroplast membranes and allowing for intracellular components including some proteins to leak out, hence the decrease in protein concentration in comparison to the non-treated plants (Qian et al., 2009). A slight outlier may exist within the treated groups protein concentrations as one of the groups provided a negative value for protein concentration which is not valid, but even after exclusion of that data value, results are still supportive of the expected outcome. Though these results support the claim of Paraquat toxicity causing membrane deterioration and leakiness, protein concentration values are rather more purposeful when used to analyze malondialdehyde (MDA) values on per mg of protein

Rubisco is the most abundant protein on earth that is essential for carbon fixation in plants. For the protein to function at its optimal level, it needs to be isolated from the mixture of proteins and in its purest form. The three isolation techniques carried out in this lab are salting out, ion exchange chromatography, and SDS-PAGE. Rubisco will be purer as each technique is conducted and will be in its purest form after the last isolation technique is carried out.

Moreover, CtXynGH30 also displayed activity against the polysaccharides having xylan main chain decorated with arabinose side chains such as arabinoxylans. Therefore a range of substrates showing the enzyme activities were treated with CtXynGH30 and the hydrolysed products were analyzed by TLC. The results showed that the enzyme is active against different polysaccharides and produces a series of oligosaccharides. The enzyme is active on xylan main chain polysaccharide substrates like beechwood-, birchwood- and 4-O-methyl glucurono-xylan and capable of releasing oligosaccharides such as xylose, xylobiose and other higher neutral and acidic oligosaccharides (Lane 1-3, Fig. 5). CtXynGH30 also acted over substrates having xylan main chain decorated with various degrees of arabinose side chains like oat spelt xylan, wheat arabinoxylan and rye arabinoxylan and producing xylobiose, xylotriose and other higher oligosaccharides (Lane 4-6, Fig. 5). Furthermore, the TLC profile of CtXynGH30 showed hydrolysis of arabinogalactan and more likely the release of arabino- oligosaccharides (Lane 7, Fig. 5), whereas, arabinan (sugar beet) and xyloglucan did not release any hydrolysed product (Lane 8-9, Fig. 5). The ability of CtXynGH30 to hydrolyse arabinoxylans apart from glucuronoxylans

BLAST search and multiple cycle alignment of OsHsfC1b (Os01g53220) show that homologous proteins are found in other monocots such as sorghum, maize and Brachypodium, but also in the dicot Arabidopsis. In rice, OsHsfC1b shares highest similarity with OsHsfC1a, another member of the four class C HSFs identified in rice (Arvidsson et al, 2008, p. 211). Proteins hold a well preserved N-terminal DNA- binding domains that has four β-sheets and α-helices and a highly conserved oligomerization domain also known as HR-A/B domain. Putative nuclear localization signal upstream of the oligomerization domain was found in all proteins (Gupta, Palma, & Corpas, 2016). A subcellular localization study was conducted to confirm targeting of OsHsfC1b to the nucleus in Arabidopsis mesophyll cell protoplast.

Enzymes are very specific protein because they contain one active site on their surface that

Arana, M. V., Sánchez-Lamas, M., Strasser, B., Ibarra, S. E., Cerdán, P. D., Botto, J. F., & Sánchez, R. A. (2014). Functional diversity of phytochrome family in the control

Boss, P. K.; Davies, C., and Robinson, S. P. Expression of anthocyanin biosynthesis pathway genes in red and white grapes. Plant Mol Biol. 1996 Nov; 32(3):565-9.

Jean Helgeson, David McCulloch, Nelson Rich, and Mary Weis. Collin College Biology 1406/1408 Lab Manual. Plano: Collin College, 2011. 76-90. Print.

Introduction Proteins are critical components in understanding cells and organisms which can contribute to further developments in medicine. Proteins compose more than 50% of the dry weight of cells [2]. Enzymes are the proteins that catalyze most reactions in a cell that keeps the cell going. By isolating protein scientists can understand, modify, and sequence specific proteins away from other cellular components. The specific protein being looked at is Rubisco (Ribulose-1,5-bisphosphate carboxylase/ oxygenase) which is a plant enzyme that has a key role in photosynthesis [1].

Campbell, N. A., & Reece, J. B. (2011). Campbell Biology. San Francisco, Calif: Benjamin Cummings.

Corn (Zea mays) is one of the most widely produced crops in the United States and it provides more than 40% of the world’s corn (Benson and Gibson). The history of maize dates back to around 5,000 - 6,000 years ago due to the Native Americans domesticating the maize ancestor. In recent years and after countless research, scientists are accepting the theory that corn comes from a wild plant called Teosinte. The reason behind the skepticism is due to the traits of both plants; teosinte possess smaller cobs, fewer rows of kernels and it has a smaller size overall. While it might seem plausible that it is part of the maize family, it did not have enough similarities to proclaim it as the ancestor of maize. However, thanks to works of multiple scientists

XhoI is a type I restriction enzyme, so the location of the recognition site on lambda DNA is unknown but it is known that it cleaves at CTCGAG sites (XhoI (10u/ul)). While the DNA fragment lengths and cleavage sites are known for HindIII lambda DNA digest, they are not known for a XhoI lambda DNA digest. The goal of this study is to determine the recognition site of XhoI on lambda DNA by comparing the DNA fragments from a HindIII digest to the DNA fragments of a HindIII and XhoI digest. We will do this by creating a mixture of solutions containing only DNA, DNA and HindIII, DNA and XhoI, and DNA, HindIII and XhoI. We will then run a gel electrophoresis, which will separate the DNA, fragments by size and we will compare the DNA fragments from each solution. Through comparing the DNA fragments from the HindIII digest and the HindIII and XhoI double digest, we will be able to determine the XhoI recognition site on the lambda DNA.

The most frequently used heme peroxidase in the enzymatic oligomerization/polymerization of arylamines is isolated from the roots of horseradish (Armoracia rusticana) and belongs to the class III family of secretory plant peroxidases (Veitch, 2004). Similarly to all other heme peroxidases, horseradish peroxidase (HRP) has an iron(III) protoporphyrin IX prosthetic group located at the active site (Veitch, 2004), Fig. 1. The most abundant isoenzyme of HRP is HRP C (Veitch, 2004), Fig. 2. For HRP C the catalytic mechanism for the oxidation of arylamines (ArNH2) at the expense of hydrogen peroxide (H2O2) is the same, the so-called “peroxidase cycle” (Veitch, 2004), Fig. 3. Following the two-electron oxidation of the native Fe(III) enzyme in the

The chemical and reagents used for the extraction and quantitation of DNA were: Plant DNAzol (0.3ml/0.1g), 100% ethanol (100%: 0.225 ml/0.1 g, 75%: 0.3 ml/0.1 g), Chloroform (0.3 ml/0.1 g), Plant DNAzol-ethanol solution: Plant DNAzol, 100% ethanol (1:0.75 v/v), TE buffer (10 mM Tris, 1 mM EDTA pH 8.0), 1.2% agarose gel (Agarose, 1X TAE buffer), 6X loading buffer (glycerol, Tris/EDTA pH 8.0, ethidium bromide), .25X TAE buffer, Restriction enzymes and Restriction endonuclease buffers. All the chemicals used were quality grade. The restriction