In:
FEBS Letters, Wiley, Vol. 356, No. 2-3 ( 1994-12-19), p. 367-371
Abstract:
A new type of peridinin—chlorophyll a protein (PCP) was isolated from the marine dinoflagellate Alexandrium cohorticula . Unlike previous studies, PCP was obtained as a single component in the presence of a protease inhibitor. The monomer had a molecular mass of 37 kDa with 12 peridinin molecules associated with 2 chl a molecules. This pigment content was much higher than that reported previously. We observed a partial amino acid sequence of the N‐terminus that is novel among photosynthetic pigment—protein complexes. Magnetic circular dichroism clearly indicated that chl a in PCP had monomeric features. Multiple spectral components were suggested for both chl a and peridinin. Based on the high pigment content, the optical properties were compared with those for a reported PCP containing 4 chl a and 1 peridinin.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(94)01314-4
Language:
English
Publisher:
Wiley
Publication Date:
1994
detail.hit.zdb_id:
1460391-3
SSG:
12
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