Jr. Reinfelder et al., RELEASE RATES OF TRACE-ELEMENTS AND PROTEIN FROM DECOMPOSING PLANKTONIC DEBRIS .2. COPEPOD CARCASSES AND SEDIMENT TRAP PARTICULATE MATTER, Journal of marine research, 51(2), 1993, pp. 423-442
In experiments designed to relate the release kinetics of various elem
ents with that of protein from biogenic particles, Ag-110m, Am-241, Cd
-109, Co-60, Se-75 and protein were measured over time in radiolabeled
copepod carcasses and particles caught in unpoisoned sediment traps (
mostly zooplankton fecal pellets and amorphous marine snow). Log-linea
r release rate constants (k) of Ag=110m, Am-241, Cd-109, and Co-60 fro
m carcasses ranged from 0.079 d-1 for Co-60 at 2-degrees-C to 0.130 d-
1 for Cd-109 at 15-degrees-C, and did not vary significantly with temp
erature. Se-75 was lost most rapidly from copepod carcasses at 2-degre
es-C, with k = 0.168 d-1; however, at 15-degrees-C, Se-75 was in two c
ompartments, with 56% in a rapidly exchanging pool (k = 0.391 d-1) and
44% in a slowly exchanging pool (k = 0.107 d-1). Protein displayed lo
ss from two compartments at both temperatures. At 2-degrees-C, protein
was lost slowly (k = 0.065 d-1) for 1 wk, after which it was released
from the carcasses very rapidly (k = 0.245 d-1). At 15-degrees-C, how
ever, the loss of protein from carcasses was more rapid over the first
2 d (k = 0.627 d-1) than thereafter (k = 0.127 d-1). The k values of
Ag-110m, Am-241, and Co-60 from sediment trap particles (15-degrees-C)
ranged from 0.008 to 0.011 d-1. Protein was lost twice as fast as Ag-
110m, Am-241, and Co-60, more slowly than half of the particulate Cd-1
09 and Se-75 in rapidly exchanging pools (k = 0.168 and 0.237 d-1, res
pectively), and at rates comparable to Cd-109 and Se-75 in slowly exch
anging pools. Overall, copepod carcasses and fecal pellets could act a
s vectors of these five elements and protein to the deep ocean, the ve
rtical flux being dependent on settling velocity and water column temp
erature structure. Of the elements considered here, Se follows the cyc
ling of protein most closely.