Human Protein Fractions Research Articles

Proteome-Wide Fragment-Based Ligand and Target Discovery.

Chemical probes are invaluable tools to investigate biological processes and can serve as lead molecules for the development of new therapies. However, despite their utility, only a fraction of human proteins have selective chemical probes, and more generally, our knowledge of the "chemically-tractable" proteome is limited, leaving many potential therapeutic targets unexploited. To help address these challenges, powerful chemical proteomic approaches have recently been developed to globally survey the ability of proteins to bind small molecules (i. e., ligandability) directly in native systems. In this review, we discuss the utility of such approaches, with a focus on the integration of chemoproteomic methods with fragment-based ligand discovery (FBLD), to facilitate the broad mapping of the ligandable proteome while also providing starting points for progression into lead chemical probes.

HPREP: a comprehensive database for human proteome repeats.

Amino acid repeats are found to play important roles in both structures and functions of the proteins. These are commonly found in all kingdoms of life, especially in eukaryotes and a larger fraction of human proteins composed of repeats. Further, the abnormal expansions of shorter repeats cause various diseases to humans. Therefore, the analysis of repeats of the entire human proteome along with functional, mutational and disease information would help to better understand their roles in proteins. To fulfill this need, we developed a web database HPREP (http://bioinfo.bdu.ac.in/hprep) for human proteome repeats using Perl and HTML programming. We identified different categories of well-characterized repeats and domain repeats that are present in the human proteome of UniProtKB/Swiss-Prot by using in-house Perl programming and novel repeats by using the repeat detection T-REKS tool as well as XSTREAM web server. Further, these proteins are annotated with functional, mutational and disease information and grouped according to specific repeat types. The developed database enables the users to search by specific repeat type in order to understand their involvement in proteins. Thus, the HPREP database is expected to be a useful resource to gain better insight regarding the different repeats in human proteome and their biological roles.

A controlled trial comparing human plasma protein fraction with freeze-dried plasma for resuscitation during the burn shock period

A controlled trial was conducted comparing the use of freeze-dried plasma (FDP) with human protein fraction (HPPF) in the resuscitation of patients during the burn shock period. Twenty-four children and 13 adults were studied during the first week post burn. It was found that those who received HPPF tended to have depressed globulin levels: the immunoglobulin levels were depressed, the prothrombin time was prolonged and the fibrinogen level was also transiently decreased. In contrast those who received FDP had raised immunoglobulin levels and the prothrombin time was shortened. The incidence of septicaemia was markedly greater during the first week if HPPF was used. The differences between the two solutions were most marked in the more extensive burns. Although the physical properties of HPPF enable it to suffice as a plasma expander, it lacks certain physiological properties of FDP. The superiority of FDP over HPPF in the resuscitation of major burns is emphasized.

Determination of Nonfibrin Protein in Fibrin Clots by Use of I131-Labeled Protein Fractions

Abstract The amount of nonfibrin proteins occluded within fibrin clots was investigated with specific radioiodinated human protein fractions. Vigorous washing of the clot followed by syneresis on absorbant paper removed all but small traces of albumin and alpha and gamma globulins. These fractions constituted approximately 6% of the total proteins in fibrin clots when fibrinogen concentrations were normal. The percentage of occluded protein increased as fibrinogen levels decreased. At fibrinogen concentrations of 48 mg./100 ml. plasma, albumin approached 20% of the total. Fibrinogen determinations which are based on the protein content, or dry weight, of the isolated clot are thus subject to systematic error which varies inversely with the fibrinogen concentration.