partial sequence information
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2020 ◽  
Vol 2020 ◽  
pp. 1-7
Author(s):  
Qingyu Cui ◽  
Yi Cao ◽  
Wenzheng Bao ◽  
Bin Yang ◽  
Yuehui Chen

In the recent years, the subject of Golgi classification has been studied intensively. It has been scientifically proven that Golgi can synthesize many substances, such as polysaccharides, and it can also combine proteins with sugars or lipids with glycoproteins and lipoproteins. In some cells (such as liver cells), the Golgi apparatus is also involved in the synthesis and secretion of lipoproteins. Therefore, the loss of Golgi protein function may have severe effects on the human body. For example, Alzheimer’s disease and diabetes are related to the loss of Golgi protein function. Because the classification of Golgi proteins has a specific effect on the treatment of these diseases, many scholars have studied the classification of Golgi proteins, but the data sets they used were complete Golgi sequences. The focus of this article is whether there is redundancy in the Golgi protein classification or, in other words, whether a part of the entire Golgi protein sequence can be used to complete the Golgi protein classification. Besides, we have adopted a new method to deal with the problem of sample imbalance. After experiments, our model has certain observability.


1979 ◽  
Vol 34 (5) ◽  
pp. 736-743 ◽  
Author(s):  
Michael Przybylski ◽  
Ingo Lüderwald ◽  
Ekkehard Kraas ◽  
Wolfgang Voelter ◽  
Sidney D. Nelson

Oligopeptides comprising the sequence of the C-terminal tetrapeptide of gastrine, Trp-Met-Asp-Phe-NH2, and several derivatives of glutathione, γ-Glu-Cys(SR)-Gly, were characterized by field desorption mass spectrometry. The field desorption mass spectra obtained at various field ion emitter temperatures reveal abundant molecular ions and fragmentation reactions that yield partial sequence information. In the series of glutathione derivatives investigated, characteristic ions formed by cleavage of the γ-Glu-Cys peptide bond determine the substituent at the Cys residue and can therefore be used to identify corresponding conjugation products of drug metabolites with glutathione.


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