2019
DOI: 10.4103/jlp.jlp_120_19
|View full text |Cite
|
Sign up to set email alerts
|

An unique encounter with paraprotenemia

Abstract: This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

0
2
0

Year Published

2020
2020
2020
2020

Publication Types

Select...
1

Relationship

0
1

Authors

Journals

citations
Cited by 1 publication
(2 citation statements)
references
References 5 publications
0
2
0
Order By: Relevance
“…The precipitation of paraproteins with reagents increase the sample turbidity and lead to interference in nephelometric, turbidimetric or colorimetric analysis. Paraproteins also may interfere immunoassays by interaction with the specific antibody reagents [10]. Another mechanism is that paraproteins inhibit of three stages of fibrin formation: the proteolytic action of thrombin on fibrinogen, the aggregation of fibrin monomers, and the stabilization of fibrin by cross-linkages in the γ and α chain.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The precipitation of paraproteins with reagents increase the sample turbidity and lead to interference in nephelometric, turbidimetric or colorimetric analysis. Paraproteins also may interfere immunoassays by interaction with the specific antibody reagents [10]. Another mechanism is that paraproteins inhibit of three stages of fibrin formation: the proteolytic action of thrombin on fibrinogen, the aggregation of fibrin monomers, and the stabilization of fibrin by cross-linkages in the γ and α chain.…”
Section: Discussionmentioning
confidence: 99%
“…Another mechanism is that paraproteins inhibit of three stages of fibrin formation: the proteolytic action of thrombin on fibrinogen, the aggregation of fibrin monomers, and the stabilization of fibrin by cross-linkages in the γ and α chain. Residual fibrin masses may cause bulky gelatinous clot formation and make it difficult to separate the serum after centrifugation [10]. Thus, obtaining sufficient serum for biochemical analyses becomes difficult.…”
Section: Discussionmentioning
confidence: 99%