PMID- 10447262
OWN - NLM
STAT- MEDLINE
DCOM- 19990921
LR  - 20081121
IS  - 1059-7794 (Print)
IS  - 1059-7794 (Linking)
VI  - 14
IP  - 1
DP  - 1999
TI  - Genotyping of the three major allelic variants of the human mannose-binding
      lectin gene by denaturing gradient gel electrophoresis.
PG  - 80-3
AB  - The three major allelic variants of the mannose-binding lectin gene are
      responsible for structural defects leading to immune deficiency. The
      corresponding mutations are all located within exon 1 and result in amino acid
      substitutions in the collagenous region of the protein, which is involved in the 
      oligomerization process. We have developed a simple and efficient strategy that
      permits simultaneous genotyping of these known allelic variants of the MBL gene
      by means of a single polymerase chain reaction (PCR) reaction followed by a
      denaturing gradient gel electrophoresis (DGGE). In addition, this procedure also 
      allows for screening novel alleles due to mutations located elsewhere in the
      analyzed segment of the gene. During this study, we identified a previously
      undescribed nucleotide change in exon 1 at codon 44.
FAU - Gabolde, M
AU  - Gabolde M
AD  - Hopital Robert Debre, Inserm U458, Paris, France.
FAU - Muralitharan, S
AU  - Muralitharan S
FAU - Besmond, C
AU  - Besmond C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Hum Mutat
JT  - Human mutation
JID - 9215429
RN  - 0 (Carrier Proteins)
RN  - 0 (Collectins)
SB  - IM
MH  - Alleles
MH  - Carrier Proteins/*genetics
MH  - Collectins
MH  - Electrophoresis, Agar Gel/*methods
MH  - Genetic Predisposition to Disease
MH  - *Genetic Variation
MH  - Genotype
MH  - Humans
MH  - Polymerase Chain Reaction/methods
EDAT- 1999/08/14 10:00
MHDA- 2000/06/22 10:00
CRDT- 1999/08/14 10:00
PHST- 1999/08/14 10:00 [pubmed]
PHST- 2000/06/22 10:00 [medline]
PHST- 1999/08/14 10:00 [entrez]
AID - 10.1002/(SICI)1098-1004(1999)14:1<80::AID-HUMU10>3.0.CO;2-J [pii]
AID - 10.1002/(SICI)1098-1004(1999)14:1<80::AID-HUMU10>3.0.CO;2-J [doi]
PST - ppublish
SO  - Hum Mutat. 1999;14(1):80-3. doi:
      10.1002/(SICI)1098-1004(1999)14:1<80::AID-HUMU10>3.0.CO;2-J.