Hunter Pujols Nearly Fought Last August - RealGM Wiretap
The Los Angeles Angels have struggled over the last few years Michael Bourn Jersey , but their issues haven't been limited to the field.
During a team meeting last August, Torii Hunter had to be physically restrained from punching out Albert Pujols.
The meeting, confirmed by several sources, came after two ugly losses to the Tampa Bay Rays.
LaTroy Hawkins called for a players' only meeting after a loss on Aug. 18, sensing discord in the clubhouse. Jered Weaver and C.J. Wilson had visibly upstaged their infielders when plays didn't go their way in the pair of losses.
Hunter and Wilson had an exchange in the dugout that many teammates witnessed.
Pujols called out Weaver and Hunter during the meeting, unaware that Hunter and Wilson had already had a conversation and cleared the air.
"Albert, you'd better get your facts straight," said Hunter, who criticized Pujols for pouting all season after the first baseman responded.
Pujols told Hunter to "shut up" and Hunter charged him from across the clubhouse, having to be restrained by Hawkins and Vernon Wells. The meeting continued and Hunter went after Pujols unsuccessfully a second time.
Angels Havent Made Decision On David Murphys Option - RealGM Wiretap
The Los Angeles Angels will have to make an interesting decision on David Murphy's club option for 2016.
Murphy carries a $7 million option and the Angels have long been searching for a left-handed hitter to face right-handers, but they are in a unique financial situation.
The Angels have eight players accounting for nearly $130 million toward next season's $189 million luxury-tax threshold -- Albert Pujols, Jered Weaver, C.J. Wilson, Mike Trout, Huston Street, Erick Aybar, Joe Smith and Josh Hamilton.
"I would love to be here," Murphy said, "but I'm not going to stress about it. I know what's supposed to happen will happen. I have no control over it. All I control is going out there and playing the best that I possibly can."
Understanding The Finer Aspects Of Protein Labeling Understanding The Finer Aspects Of Protein Labeling November 26, 2013 | Author: Katrina Wheeler | Posted in Education
The role of protein labeling plays a key part in biological research and experiments to understand how molecules function. Amino acids make up protein which is an important nutrient for human beings and other living organisms alike. A selected protein may be infused with a binding partner for the process of labeling molecules.
Each area of the body functions differently and there are several different methods to get an understanding of each. For certain parts, fluorescent kits can help in this purpose. The specific area for testing largely determines the choice of the testing method.
A popular choice is biotin mainly due to its advantage of being able to bind with proteins like Neutravidin, avidin and streptavidin. Its interaction with material of a non covalent nature is effective which helps in processes like purification, detection and immobilization. The appearance of the enzyme level of biotin is smaller and intervention in its function is relatively not an issue.
Biotinylation is a process in which biotin is used in chemical and enzyme series. As reagents are similar, there is a general preference for the chemical process. In the process of labeling, three components are required which are reactive group, spacer arm and biotinyl.
With the perception of being larger to biotin, enzyme probes offer another alternative for labelling. Certain enzyme types have different reactions with specific components making them unique. With extended shelf life and being more versatile they are more effective in the detection of proteins in tissues and cells.
There is a vast range of enzyme products that can be used in various biological processes for chemists to choose from. Choices also abound in the case of the extra substrate that is needed for the signal to be generated. Enzymes also have the advantage of being suitable for antibodies apart from complicated procedures like reductive animation and crosslinking.
Another method that can also be used is the use of fluorescent molecules which react to any source of light giving off a distinct signal. They can perform by themselves without requiring any other reagents in experiments. Their discovery is recognized as a significant advancement in technology in protein purification, vivo processes and detection.
Lately the variations of fluorescent probes have increased markedly enhancing the versatility of their performance. Despite requiring equipment that is more specialized and sophisticated, they deliver superior results in this entire process from inception to completion. Therefore in comparison to the other methods of labeling, fluorescent products are a better bet.
There is need for research to keep pace with the advancing technology in molecular labeling so that the normal cell functioning is not affected. Chemists have accordingly reacted with a technique which requires a fluorophone attachment. They are smaller when compared to the regular fluorescent probes currently in use and have to be linked to another protein.
In the results a steady link emerges as the two elements react with each other which was earlier not thought possible. In the choice of protein labeling technique the compatibility factor is of prime importance. The results of a biological experiment are largely determined by which alternative is chosen.
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