PMID- 6860630
OWN - NLM
STAT- MEDLINE
DCOM- 19830817
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 22
IP  - 10
DP  - 1983 May 10
TI  - Cadmium-113 nuclear magnetic resonance studies of proteolytic fragments of 
      calmodulin: assignment of strong and weak cation binding sites.
PG  - 2309-13
AB  - Proteolytic fragments of bovine testis calmodulin were obtained by limited 
      proteolysis with trypsin or thrombin. Cadmium-113 NMR studies showed that the 
      tryptic fragment encompassing Ca2+ binding domains III and IV (TR2C) gave rise to 
      a spectrum identical with that of the native protein. Two thrombic fragments 
      containing either domains I, II, and III [TM1-(1-106)] or the single domain IV 
      [TM2-(107-148)] both gave rise to one broad resonance only. These data indicate 
      that domains III and IV comprise the two high-affinity Ca2+ binding sites in 
      intact calmodulin and that disturbance of the structural relationship between 
      domain III and domain IV markedly reduces the affinity of these two sites for 
      Ca2+ ions. These observations are discussed with respect to other published 
      accounts concerning the sequence in which the four calcium domains in calmodulin 
      are filled.
FAU - Andersson, A
AU  - Andersson A
FAU - Forsen, S
AU  - Forsen S
FAU - Thulin, E
AU  - Thulin E
FAU - Vogel, H J
AU  - Vogel HJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Calmodulin)
RN  - 0 (Cations)
RN  - 0 (Peptide Fragments)
RN  - 00BH33GNGH (Cadmium)
RN  - EC 3.4.21.4 (Trypsin)
RN  - EC 3.4.21.5 (Thrombin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Cadmium/metabolism
MH  - Calcium/*metabolism
MH  - Calcium-Binding Proteins/*metabolism
MH  - Calmodulin/*metabolism
MH  - Cations
MH  - Cattle
MH  - Kinetics
MH  - Magnetic Resonance Spectroscopy/methods
MH  - Male
MH  - Peptide Fragments/*metabolism
MH  - Protein Conformation
MH  - Testis
MH  - Thrombin
MH  - Trypsin
EDAT- 1983/05/10 00:00
MHDA- 1983/05/10 00:01
CRDT- 1983/05/10 00:00
PHST- 1983/05/10 00:00 [pubmed]
PHST- 1983/05/10 00:01 [medline]
PHST- 1983/05/10 00:00 [entrez]
AID - 10.1021/bi00279a001 [doi]
PST - ppublish
SO  - Biochemistry. 1983 May 10;22(10):2309-13. doi: 10.1021/bi00279a001.