PMID- 2938950
OWN - NLM
STAT- MEDLINE
DCOM- 19860618
LR  - 20191210
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 156
IP  - 3
DP  - 1986 May 2
TI  - Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of 
      calsequestrin and of parvalbumin in rabbit skeletal muscles of defined fiber 
      composition.
PG  - 489-96
AB  - Antibodies directed against purified Ca-ATPase from sarcoplasmic reticulum, 
      calsequestrin and parvalbumin from rabbit fast-twitch muscle were raised in 
      sheep. The specificity of the antibodies was shown by immunoblot analysis and by 
      enzyme-linked immunoadsorbent assays (ELISAs). IgG against the sarcoplasmic 
      reticulum Ca-ATPase inhibited the catalytic activities of Ca-ATPase from 
      fast-twitch (psoas, tibialis anterior) and slow-twitch (soleus) muscles to the 
      same degree. In non-equilibrium competitive ELISAs the anti(Ca-ATPase) IgG 
      displayed a slightly higher affinity for the Ca-ATPase from fast-twitch muscle 
      than for that from slow-twitch muscle. This suggests a fiber-type-specific 
      polymorphism of the sarcoplasmic reticulum Ca-ATPase. Quantification of 
      Ca-ATPase, calsequestrin and parvalbumin in various rabbit skeletal muscles of 
      histochemically determined fiber composition was achieved by sandwich ELISA. 
      Ca-ATPase was found to be 6-7 times higher in fast than in slow-twitch muscles. A 
      slightly higher concentration was found in fast-twitch muscles with a higher 
      percentage of IIb fibers when compared with fast-twitch muscles with a higher 
      percentage of IIa fibers. Thus Ca-ATPase is distributed as follows, IIb greater 
      than or equal to IIa much greater than I. Calsequestrin was uniformly distributed 
      in fast-twitch muscles independently of their IIa/IIb fiber ratio and displayed 
      50% lower concentrations in slow than in fast-twitch muscles (IIb = IIa greater 
      than I). Parvalbumin contents were 200-300-fold higher in fast than in 
      slow-twitch muscles. Significantly lower parvalbumin concentrations were found in 
      fast-twitch muscles with a higher percentage of IIa fibers than in fast-twitch 
      muscles with a higher percentage of IIb fibers (IIb greater than IIa much greater 
      than I).
FAU - Leberer, E
AU  - Leberer E
FAU - Pette, D
AU  - Pette D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Calsequestrin)
RN  - 0 (Muscle Proteins)
RN  - 0 (Parvalbumins)
RN  - EC 7.2.2.10 (Calcium-Transporting ATPases)
SB  - IM
MH  - Animals
MH  - Antibody Specificity
MH  - Calcium-Transporting ATPases/*isolation & purification
MH  - Calsequestrin/*isolation & purification
MH  - Enzyme-Linked Immunosorbent Assay/methods
MH  - Immunochemistry
MH  - Muscle Proteins/*isolation & purification
MH  - Muscles/*analysis/anatomy & histology/enzymology
MH  - Parvalbumins/*isolation & purification
MH  - Rabbits
MH  - Sarcoplasmic Reticulum/analysis/enzymology
EDAT- 1986/05/02 00:00
MHDA- 1986/05/02 00:01
CRDT- 1986/05/02 00:00
PHST- 1986/05/02 00:00 [pubmed]
PHST- 1986/05/02 00:01 [medline]
PHST- 1986/05/02 00:00 [entrez]
AID - 10.1111/j.1432-1033.1986.tb09607.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1986 May 2;156(3):489-96. doi: 10.1111/j.1432-1033.1986.tb09607.x.